ID FNBP4_HUMAN Reviewed; 1017 AA. AC Q8N3X1; Q9H985; Q9NT81; Q9Y2L7; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 3. DT 27-MAR-2024, entry version 162. DE RecName: Full=Formin-binding protein 4; DE AltName: Full=Formin-binding protein 30; GN Name=FNBP4; Synonyms=FBP30, KIAA1014; 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 [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [2] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1017 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 457-1017 (ISOFORMS 1/2). 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 [7] RP INTERACTION WITH KHDRBS1. RX PubMed=10748127; DOI=10.1074/jbc.m909368199; RA Bedford M.T., Frankel A., Yaffe M.B., Clarke S., Leder P., Richard S.; RT "Arginine methylation inhibits the binding of proline-rich ligands to Src RT homology 3, but not WW, domains."; RL J. Biol. Chem. 275:16030-16036(2000). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-172, AND RP IDENTIFICATION BY 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-432; SER-963; RP SER-964 AND SER-965, 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 [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; SER-435 AND SER-499, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-116; SER-432; RP SER-464; THR-479 AND SER-508, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-508, AND RP IDENTIFICATION BY 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 [16] RP TISSUE SPECIFICITY, AND VARIANT MET-228. RX PubMed=23703728; DOI=10.1002/ajmg.a.35983; RA Kondo Y., Koshimizu E., Megarbane A., Hamanoue H., Okada I., Nishiyama K., RA Kodera H., Miyatake S., Tsurusaki Y., Nakashima M., Doi H., Miyake N., RA Saitsu H., Matsumoto N.; RT "Whole-exome sequencing identified a homozygous FNBP4 mutation in a family RT with a condition similar to microphthalmia with limb anomalies."; RL Am. J. Med. Genet. A 161A:1543-1546(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-116; SER-432; RP THR-479; SER-499; SER-508; THR-516 AND THR-517, AND IDENTIFICATION BY MASS RP 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 [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-348 AND LYS-519, AND RP IDENTIFICATION BY MASS 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-301; LYS-348 AND LYS-519, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-348, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-335; LYS-348 AND LYS-519, 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). CC -!- SUBUNIT: Binds FMN1. Interacts with the Arg/Gly-rich-flanked Pro-rich CC of KHDRBS1/SAM68. Arginine methylation in these regions has no effect CC on this binding. {ECO:0000269|PubMed:10748127}. CC -!- INTERACTION: CC Q8N3X1; P42858: HTT; NbExp=6; IntAct=EBI-310600, EBI-466029; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8N3X1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N3X1-2; Sequence=VSP_040292; CC -!- TISSUE SPECIFICITY: Highly expressed in the eye. CC {ECO:0000269|PubMed:23703728}. CC -!- DOMAIN: These WW domains interact with Arg/Gly-rich-flanked Pro-rich CC domains found in several WW domain-binding proteins (WBPs). The N- CC terminal WW domain has the greater ligand-binding ability (By CC similarity). {ECO:0000250}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA76858.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AB023231; BAA76858.2; ALT_INIT; mRNA. DR EMBL; AC021443; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC037404; AAH37404.1; -; mRNA. DR EMBL; AL137480; CAB70761.1; -; mRNA. DR EMBL; AK022987; BAB14348.1; -; mRNA. DR CCDS; CCDS41644.1; -. [Q8N3X1-1] DR PIR; T46422; T46422. DR RefSeq; NP_001305268.1; NM_001318339.1. [Q8N3X1-2] DR RefSeq; NP_056123.2; NM_015308.3. [Q8N3X1-1] DR AlphaFoldDB; Q8N3X1; -. DR SMR; Q8N3X1; -. DR BioGRID; 116941; 63. DR DIP; DIP-31674N; -. DR IntAct; Q8N3X1; 12. DR MINT; Q8N3X1; -. DR STRING; 9606.ENSP00000263773; -. DR GlyCosmos; Q8N3X1; 16 sites, 2 glycans. DR GlyGen; Q8N3X1; 18 sites, 2 O-linked glycans (18 sites). DR iPTMnet; Q8N3X1; -. DR MetOSite; Q8N3X1; -. DR PhosphoSitePlus; Q8N3X1; -. DR BioMuta; FNBP4; -. DR DMDM; 313104235; -. DR EPD; Q8N3X1; -. DR jPOST; Q8N3X1; -. DR MassIVE; Q8N3X1; -. DR MaxQB; Q8N3X1; -. DR PaxDb; 9606-ENSP00000263773; -. DR PeptideAtlas; Q8N3X1; -. DR ProteomicsDB; 71841; -. [Q8N3X1-1] DR ProteomicsDB; 71842; -. [Q8N3X1-2] DR Pumba; Q8N3X1; -. DR Antibodypedia; 26877; 63 antibodies from 17 providers. DR DNASU; 23360; -. DR Ensembl; ENST00000263773.10; ENSP00000263773.5; ENSG00000109920.13. [Q8N3X1-1] DR Ensembl; ENST00000646180.2; ENSP00000494562.1; ENSG00000285182.2. [Q8N3X1-1] DR GeneID; 23360; -. DR KEGG; hsa:23360; -. DR MANE-Select; ENST00000263773.10; ENSP00000263773.5; NM_015308.5; NP_056123.2. DR UCSC; uc009ylv.4; human. [Q8N3X1-1] DR AGR; HGNC:19752; -. DR CTD; 23360; -. DR DisGeNET; 23360; -. DR GeneCards; FNBP4; -. DR HGNC; HGNC:19752; FNBP4. DR HPA; ENSG00000109920; Low tissue specificity. DR MIM; 615265; gene. DR neXtProt; NX_Q8N3X1; -. DR OpenTargets; ENSG00000109920; -. DR PharmGKB; PA134971679; -. DR VEuPathDB; HostDB:ENSG00000109920; -. DR eggNOG; ENOG502QTDD; Eukaryota. DR GeneTree; ENSGT00390000003450; -. DR HOGENOM; CLU_015402_0_0_1; -. DR InParanoid; Q8N3X1; -. DR OMA; AYWGIPA; -. DR OrthoDB; 3093715at2759; -. DR PhylomeDB; Q8N3X1; -. DR TreeFam; TF331046; -. DR PathwayCommons; Q8N3X1; -. DR SignaLink; Q8N3X1; -. DR BioGRID-ORCS; 23360; 377 hits in 1166 CRISPR screens. DR ChiTaRS; FNBP4; human. DR GeneWiki; FNBP4; -. DR GenomeRNAi; 23360; -. DR Pharos; Q8N3X1; Tdark. DR PRO; PR:Q8N3X1; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q8N3X1; Protein. DR Bgee; ENSG00000109920; Expressed in sural nerve and 136 other cell types or tissues. DR ExpressionAtlas; Q8N3X1; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR CDD; cd00201; WW; 2. DR Gene3D; 2.20.70.10; -; 2. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR46697; FORMIN-BINDING PROTEIN 4; 1. DR PANTHER; PTHR46697:SF1; FORMIN-BINDING PROTEIN 4; 1. DR Pfam; PF00397; WW; 2. DR SMART; SM00456; WW; 2. DR SUPFAM; SSF51045; WW domain; 2. DR PROSITE; PS01159; WW_DOMAIN_1; 1. DR PROSITE; PS50020; WW_DOMAIN_2; 2. DR Genevisible; Q8N3X1; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Isopeptide bond; Phosphoprotein; KW Reference proteome; Repeat; Ubl conjugation. FT CHAIN 1..1017 FT /note="Formin-binding protein 4" FT /id="PRO_0000289863" FT DOMAIN 214..248 FT /note="WW 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 595..629 FT /note="WW 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT REGION 1..141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 160..202 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 421..519 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 621..676 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 706..792 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 899..994 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 41..66 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 163..178 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 181..202 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 428..445 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 462..480 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 490..519 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 624..639 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 652..676 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 706..734 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 736..752 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 760..792 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 901..924 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 116 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 124 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6ZQ03" FT MOD_RES 172 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 290 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q6ZQ03" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6ZQ03" FT MOD_RES 432 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 435 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 438 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6ZQ03" FT MOD_RES 442 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6ZQ03" FT MOD_RES 464 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 479 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 499 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 508 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 516 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 517 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 963 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 964 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 965 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 301 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 335 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 348 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 348 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 519 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 519 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 73 FT /note="E -> EGK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10231032" FT /id="VSP_040292" FT VARIANT 125 FT /note="E -> G (in dbSNP:rs34962598)" FT /id="VAR_032623" FT VARIANT 228 FT /note="T -> M (found in a patient with microphthalmia with FT limb anomalies; uncertain significance; dbSNP:rs780064080)" FT /evidence="ECO:0000269|PubMed:23703728" FT /id="VAR_075345" FT VARIANT 794 FT /note="T -> A (in dbSNP:rs35040940)" FT /id="VAR_032624" FT CONFLICT 55..56 FT /note="Missing (in Ref. 1; BAA76858, 4; AAH37404 and 5; FT CAB70761)" FT /evidence="ECO:0000305" SQ SEQUENCE 1017 AA; 110266 MW; 510DC8011B5973AD CRC64; MGKKSRAVPG RRPILQLSPP GPRGSTPGRD PEPEPDTEPD STAAVPSQPA PSAATTTTTA VTAAAASDDS PSEDEQEAVQ EVPRVVQNPP KPVMTTRPTA VKATGGLCLL GAYADSDDDD NDVSEKLAQS KETNGNQSTD IDSTLANFLA EIDAITAPQP AAPVGASAPP PTPPRPEPKE AATSTLSSST SNGTDSTQTS GWQYDTQCSL AGVGIEMGDW QEVWDENTGC YYYWNTQTNE VTWELPQYLA TQVQGLQHYQ PSSVPGAETS FVVNTDIYSK EKTISVSSSK SGPVIAKREV KKEVNEGIQA LSNSEEEKKG VAASLLAPLL PEGIKEEEER WRRKVICKEE PVSEVKETST TVEEATTIVK PQEIMLDNIE DPSQEDLCSV VQSGESEEEE EQDTLELELV LERKKAELRA LEEGDGSVSG SSPRSDISQP ASQDGMRRLM SKRGKWKMFV RATSPESTSR SSSKTGRDTP ENGETAIGAE NSEKIDENSD KEMEVEESPE KIKVQTTPKV EEEQDLKFQI GELANTLTSK FEFLGINRQS ISNFHVLLLQ TETRIADWRE GALNGNYLKR KLQDAAEQLK QYEINATPKG WSCHWDRDHR RYFYVNEQSG ESQWEFPDGE EEEEESQAQE NRDETLAKQT LKDKTGTDSN STESSETSTG SLCKESFSGQ VSSSSLMPLT PFWTLLQSNV PVLQPPLPLE MPPPPPPPPE SPPPPPPPPP PAEDGEIQEV EMEDEGSEEP PAPGTEEDTP LKPSAQTTVV TSQSSVDSTI SSSSSTKGIK RKATEISTAV VQRSATIGSS PVLYSQSAIA TGHQAAGIGN QATGIGHQTI PVSLPAAGMG HQARGMSLQS NYLGLAAAPA IMSYAECSVP IGVTAPSLQP VQARGAVPTA TIIEPPPPPP PPPPPPPPAP KMPPPEKTKK GRKDKAKKSK TKMPSLVKKW QSIQRELDEE DNSSSSEEDR ESTAQKRIEE WKQQQLVSGM AERNANFEAL PEDWRARLKR RKMAPNT //