FNBP4_HUMAN
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 03-AUG-2022, entry version 153.
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};
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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; 53.
DR DIP; DIP-31674N; -.
DR IntAct; Q8N3X1; 13.
DR MINT; Q8N3X1; -.
DR STRING; 9606.ENSP00000263773; -.
DR GlyGen; Q8N3X1; 16 sites, 2 O-linked glycans (16 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; Q8N3X1; -.
DR PeptideAtlas; Q8N3X1; -.
DR PRIDE; Q8N3X1; -.
DR ProteomicsDB; 71841; -. [Q8N3X1-1]
DR ProteomicsDB; 71842; -. [Q8N3X1-2]
DR Antibodypedia; 26877; 50 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 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; QSAGIGH; -.
DR OrthoDB; 472232at2759; -.
DR PhylomeDB; Q8N3X1; -.
DR TreeFam; TF331046; -.
DR PathwayCommons; Q8N3X1; -.
DR SignaLink; Q8N3X1; -.
DR BioGRID-ORCS; 23360; 366 hits in 1083 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 134 other tissues.
DR ExpressionAtlas; Q8N3X1; baseline and differential.
DR Genevisible; Q8N3X1; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR CDD; cd00201; WW; 2.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
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 (rare variant found in a patient with
FT microphthalmia with limb anomalies; unknown pathological
FT 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
