ID   LIPB1_HUMAN             Reviewed;        1011 AA.
AC   Q86W92; O75336; Q86X70; Q9NY03; Q9ULJ0;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Liprin-beta-1;
DE   AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 1;
DE            Short=PTPRF-interacting protein-binding protein 1;
DE   AltName: Full=hSGT2;
GN   Name=PPFIBP1; Synonyms=KIAA1230;
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 [MRNA] (ISOFORM 2), VARIANT LEU-148, TISSUE
RP   SPECIFICITY, AND FUNCTION.
RX   PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA   Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT   "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT   interacting proteins.";
RL   J. Biol. Chem. 273:15611-15620(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LEU-148.
RC   TISSUE=Brain;
RX   PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANT LEU-148.
RA   Junjian L., Cheng J., Rouli Z., Jie Z.;
RT   "L2, a different isoform of Liprin beta 1, is expressed in high level in
RT   liver tissue.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANT LEU-148.
RC   TISSUE=Brain;
RA   Sato T., Jigami Y., Uemura H.;
RT   "hSGT2, a liprin related human gene, restores the glycolytic gene
RT   expression of the gcr2 mutant of Saccharomyces cerevisiae.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP   LEU-148.
RC   TISSUE=Brain, and Skin;
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   [7]
RP   INTERACTION WITH S100A4.
RX   PubMed=11836260; DOI=10.1074/jbc.m110976200;
RA   Kriajevska M., Fischer-Larsen M., Moertz E., Vorm O., Tulchinsky E.,
RA   Grigorian M., Ambartsumian N., Lukanidin E.;
RT   "Liprin beta 1, a member of the family of LAR transmembrane tyrosine
RT   phosphatase-interacting proteins, is a new target for the metastasis-
RT   associated protein S100A4 (Mts1).";
RL   J. Biol. Chem. 277:5229-5235(2002).
RN   [8]
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-37; THR-39; SER-40; SER-466;
RP   SER-579; SER-601; SER-999; SER-1001; SER-1003 AND THR-1005, PHOSPHORYLATION
RP   [LARGE SCALE ANALYSIS] AT SER-523 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE 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-601, AND IDENTIFICATION BY
RP   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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-322, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-40; SER-999 AND
RP   SER-1001, AND 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   [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-999, 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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540; SER-601 AND SER-794, 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-540 AND SER-794, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-471, AND IDENTIFICATION BY MASS
RP   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   [19]
RP   INVOLVEMENT IN NEDSMBA, AND VARIANTS NEDSMBA 135-ARG--VAL-1011 DEL;
RP   451-GLN--VAL-1011 DEL; 507-GLN--VAL-1011 DEL; VAL-732; 811-ARG--VAL-1011
RP   DEL AND 883-ARG--VAL-1011 DEL.
RX   PubMed=35830857; DOI=10.1016/j.ajhg.2022.06.008;
RA   Rosenhahn E., O'Brien T.J., Zaki M.S., Sorge I., Wieczorek D., Rostasy K.,
RA   Vitobello A., Nambot S., Alkuraya F.S., Hashem M.O., Alhashem A.,
RA   Tabarki B., Alamri A.S., Al Safar A.H., Bubshait D.K., Alahmady N.F.,
RA   Gleeson J.G., Abdel-Hamid M.S., Lesko N., Ygberg S., Correia S.P.,
RA   Wredenberg A., Alavi S., Seyedhassani S.M., Ebrahimi Nasab M., Hussien H.,
RA   Omar T.E.I., Harzallah I., Touraine R., Tajsharghi H., Morsy H.,
RA   Houlden H., Shahrooei M., Ghavideldarestani M., Abdel-Salam G.M.H.,
RA   Torella A., Zanobio M., Terrone G., Brunetti-Pierri N., Omrani A.,
RA   Hentschel J., Lemke J.R., Sticht H., Abou Jamra R., Brown A.E.X.,
RA   Maroofian R., Platzer K.;
RT   "Bi-allelic loss-of-function variants in PPFIBP1 cause a neurodevelopmental
RT   disorder with microcephaly, epilepsy, and periventricular calcifications.";
RL   Am. J. Hum. Genet. 109:1421-1435(2022).
CC   -!- FUNCTION: May regulate the disassembly of focal adhesions. Did not bind
CC       receptor-like tyrosine phosphatases type 2A.
CC       {ECO:0000269|PubMed:9624153}.
CC   -!- SUBUNIT: Forms homodimers and heterodimers. Interacts with S100A4 in a
CC       calcium-dependent mode. {ECO:0000269|PubMed:11836260}.
CC   -!- INTERACTION:
CC       Q86W92; P40425: PBX2; NbExp=3; IntAct=EBI-1045582, EBI-348489;
CC       Q86W92; P31947: SFN; NbExp=4; IntAct=EBI-1045582, EBI-476295;
CC       Q86W92; P62258: YWHAE; NbExp=4; IntAct=EBI-1045582, EBI-356498;
CC       Q86W92; P63104: YWHAZ; NbExp=3; IntAct=EBI-1045582, EBI-347088;
CC       Q86W92; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-1045582, EBI-25492395;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q86W92-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86W92-2; Sequence=VSP_009397, VSP_009398, VSP_009399,
CC                                  VSP_009400;
CC       Name=3;
CC         IsoId=Q86W92-3; Sequence=VSP_009394;
CC       Name=4;
CC         IsoId=Q86W92-4; Sequence=VSP_009397;
CC       Name=5; Synonyms=L2;
CC         IsoId=Q86W92-5; Sequence=VSP_009395, VSP_009396;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Absent in liver.
CC       {ECO:0000269|PubMed:9624153}.
CC   -!- DOMAIN: The N-terminal coiled coil regions mediate homodimerization
CC       preferentially and heterodimerization type beta/beta. The C-terminal,
CC       non-coiled coil regions mediate heterodimerization type beta/alpha and
CC       interaction with S100A4. {ECO:0000269|PubMed:11836260}.
CC   -!- DISEASE: Neurodevelopmental disorder with seizures, microcephaly, and
CC       brain abnormalities (NEDSMBA) [MIM:620024]: An autosomal recessive
CC       disorder characterized by global developmental delay, severe to
CC       profound intellectual disability, progressive microcephaly, refractory
CC       early-onset epilepsy, white matter abnormalities, and periventricular
CC       calcifications. {ECO:0000269|PubMed:35830857}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 5]: Due to intron retention. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the liprin family. Liprin-beta subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH46159.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA86544.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF034802; AAC26103.1; -; mRNA.
DR   EMBL; AB033056; BAA86544.2; ALT_INIT; mRNA.
DR   EMBL; AJ276680; CAB77544.1; -; mRNA.
DR   EMBL; AB049149; BAB39690.1; -; mRNA.
DR   EMBL; BC046159; AAH46159.1; ALT_INIT; mRNA.
DR   EMBL; BC050281; AAH50281.1; -; mRNA.
DR   CCDS; CCDS55812.1; -. [Q86W92-1]
DR   CCDS; CCDS55813.1; -. [Q86W92-4]
DR   CCDS; CCDS55814.1; -. [Q86W92-3]
DR   CCDS; CCDS8713.1; -. [Q86W92-2]
DR   RefSeq; NP_001185844.1; NM_001198915.1. [Q86W92-3]
DR   RefSeq; NP_001185845.1; NM_001198916.1. [Q86W92-4]
DR   RefSeq; NP_003613.3; NM_003622.3. [Q86W92-2]
DR   RefSeq; NP_803193.2; NM_177444.2. [Q86W92-1]
DR   AlphaFoldDB; Q86W92; -.
DR   SMR; Q86W92; -.
DR   BioGRID; 114068; 187.
DR   DIP; DIP-42195N; -.
DR   IntAct; Q86W92; 51.
DR   MINT; Q86W92; -.
DR   STRING; 9606.ENSP00000314724; -.
DR   GlyGen; Q86W92; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q86W92; -.
DR   MetOSite; Q86W92; -.
DR   PhosphoSitePlus; Q86W92; -.
DR   BioMuta; PPFIBP1; -.
DR   DMDM; 90185247; -.
DR   EPD; Q86W92; -.
DR   jPOST; Q86W92; -.
DR   MassIVE; Q86W92; -.
DR   MaxQB; Q86W92; -.
DR   PaxDb; 9606-ENSP00000314724; -.
DR   PeptideAtlas; Q86W92; -.
DR   ProteomicsDB; 70131; -. [Q86W92-1]
DR   ProteomicsDB; 70132; -. [Q86W92-2]
DR   ProteomicsDB; 70133; -. [Q86W92-3]
DR   ProteomicsDB; 70134; -. [Q86W92-4]
DR   ProteomicsDB; 70135; -. [Q86W92-5]
DR   Pumba; Q86W92; -.
DR   Antibodypedia; 1098; 194 antibodies from 29 providers.
DR   DNASU; 8496; -.
DR   Ensembl; ENST00000228425.11; ENSP00000228425.6; ENSG00000110841.14. [Q86W92-2]
DR   Ensembl; ENST00000318304.12; ENSP00000314724.8; ENSG00000110841.14. [Q86W92-1]
DR   Ensembl; ENST00000535047.5; ENSP00000444046.1; ENSG00000110841.14. [Q86W92-5]
DR   Ensembl; ENST00000537927.5; ENSP00000445425.1; ENSG00000110841.14. [Q86W92-3]
DR   Ensembl; ENST00000542629.5; ENSP00000443442.1; ENSG00000110841.14. [Q86W92-4]
DR   GeneID; 8496; -.
DR   KEGG; hsa:8496; -.
DR   MANE-Select; ENST00000228425.11; ENSP00000228425.6; NM_003622.4; NP_003613.4. [Q86W92-2]
DR   UCSC; uc001rhz.3; human. [Q86W92-1]
DR   AGR; HGNC:9249; -.
DR   CTD; 8496; -.
DR   DisGeNET; 8496; -.
DR   GeneCards; PPFIBP1; -.
DR   HGNC; HGNC:9249; PPFIBP1.
DR   HPA; ENSG00000110841; Low tissue specificity.
DR   MalaCards; PPFIBP1; -.
DR   MIM; 603141; gene.
DR   MIM; 620024; phenotype.
DR   neXtProt; NX_Q86W92; -.
DR   OpenTargets; ENSG00000110841; -.
DR   PharmGKB; PA33570; -.
DR   VEuPathDB; HostDB:ENSG00000110841; -.
DR   eggNOG; KOG1899; Eukaryota.
DR   GeneTree; ENSGT01050000244951; -.
DR   HOGENOM; CLU_011689_2_0_1; -.
DR   InParanoid; Q86W92; -.
DR   OMA; VETQPCD; -.
DR   OrthoDB; 5396517at2759; -.
DR   PhylomeDB; Q86W92; -.
DR   TreeFam; TF314207; -.
DR   PathwayCommons; Q86W92; -.
DR   Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR   Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR   SignaLink; Q86W92; -.
DR   BioGRID-ORCS; 8496; 15 hits in 1146 CRISPR screens.
DR   ChiTaRS; PPFIBP1; human.
DR   GeneWiki; PPFIBP1; -.
DR   GenomeRNAi; 8496; -.
DR   Pharos; Q86W92; Tbio.
DR   PRO; PR:Q86W92; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q86W92; Protein.
DR   Bgee; ENSG00000110841; Expressed in tendon of biceps brachii and 207 other cell types or tissues.
DR   ExpressionAtlas; Q86W92; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR   CDD; cd09563; SAM_liprin-beta1_2_repeat1; 1.
DR   CDD; cd09566; SAM_liprin-beta1_2_repeat2; 1.
DR   CDD; cd09569; SAM_liprin-beta1_2_repeat3; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 3.
DR   InterPro; IPR029515; Liprin.
DR   InterPro; IPR037617; Liprin-beta_SAM_rpt_1.
DR   InterPro; IPR037618; Liprin-beta_SAM_rpt_2.
DR   InterPro; IPR037619; Liprin-beta_SAM_rpt_3.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR12587; LAR INTERACTING PROTEIN LIP -RELATED PROTEIN; 1.
DR   PANTHER; PTHR12587:SF16; LIPRIN-BETA-1; 1.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
DR   Genevisible; Q86W92; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Disease variant; Epilepsy;
KW   Intellectual disability; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..1011
FT                   /note="Liprin-beta-1"
FT                   /id="PRO_0000191034"
FT   DOMAIN          647..711
FT                   /note="SAM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          719..782
FT                   /note="SAM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          804..876
FT                   /note="SAM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          420..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          156..405
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        472..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         39
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         322
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C8U0"
FT   MOD_RES         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         579
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         601
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         636
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C8U0"
FT   MOD_RES         794
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         999
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         1001
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         1003
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1005
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CROSSLNK        471
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..153
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10574462"
FT                   /id="VSP_009394"
FT   VAR_SEQ         158..170
FT                   /note="ELLSRTSLETQKL -> VCAEARTKMGFPC (in isoform 5)"
FT                   /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT                   /id="VSP_009395"
FT   VAR_SEQ         171..1011
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT                   /id="VSP_009396"
FT   VAR_SEQ         233..263
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9624153"
FT                   /id="VSP_009397"
FT   VAR_SEQ         302
FT                   /note="D -> DENFKKKLKEKN (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9624153"
FT                   /id="VSP_009398"
FT   VAR_SEQ         349
FT                   /note="K -> KKGK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9624153"
FT                   /id="VSP_009399"
FT   VAR_SEQ         544
FT                   /note="L -> LDRKRSASAPTL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9624153"
FT                   /id="VSP_009400"
FT   VARIANT         135..1011
FT                   /note="Missing (in NEDSMBA)"
FT                   /evidence="ECO:0000269|PubMed:35830857"
FT                   /id="VAR_087715"
FT   VARIANT         148
FT                   /note="V -> L (in dbSNP:rs2194816)"
FT                   /evidence="ECO:0000269|PubMed:10574462,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9624153,
FT                   ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT                   /id="VAR_017758"
FT   VARIANT         451..1011
FT                   /note="Missing (in NEDSMBA)"
FT                   /evidence="ECO:0000269|PubMed:35830857"
FT                   /id="VAR_087716"
FT   VARIANT         507..1011
FT                   /note="Missing (in NEDSMBA)"
FT                   /evidence="ECO:0000269|PubMed:35830857"
FT                   /id="VAR_087717"
FT   VARIANT         732
FT                   /note="G -> V (in NEDSMBA; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:35830857"
FT                   /id="VAR_087718"
FT   VARIANT         811..1011
FT                   /note="Missing (in NEDSMBA)"
FT                   /evidence="ECO:0000269|PubMed:35830857"
FT                   /id="VAR_087719"
FT   VARIANT         883..1011
FT                   /note="Missing (in NEDSMBA)"
FT                   /evidence="ECO:0000269|PubMed:35830857"
FT                   /id="VAR_087720"
FT   CONFLICT        308
FT                   /note="M -> K (in Ref. 6; AAH46159)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        453
FT                   /note="C -> R (in Ref. 1; AAC26103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        553
FT                   /note="E -> A (in Ref. 1; AAC26103)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q86W92-2:523
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
SQ   SEQUENCE   1011 AA;  114024 MW;  20E30DD99ACD5A92 CRC64;
     MMSDASDMLA AALEQMDGII AGSKALEYSN GIFDCQSPTS PFMGSLRALH LVEDLRGLLE
     MMETDEKEGL RCQIPDSTAE TLVEWLQSQM TNGHLPGNGD VYQERLARLE NDKESLVLQV
     SVLTDQVEAQ GEKIRDLEFC LEEHREKVNA TEEMLQQELL SRTSLETQKL DLMAEISNLK
     LKLTAVEKDR LDYEDKFRDT EGLIQEINDL RLKVSEMDSE RLQYEKKLKS TKSLMAKLSS
     MKIKVGQMQY EKQRMEQKWE SLKDELASLK EQLEEKESEV KRLQEKLVCK MKGEGVEIVD
     RDIEVQKMKK AVESLMAANE EKDRKIEDLR QCLNRYKKMQ DTVVLAQGKD GEYEELLNSS
     SISSLLDAQG FSDLEKSPSP TPVMGSPSCD PFNTSVPEEF HTTILQVSIP SLLPATVSME
     TSEKSKLTPK PETSFEENDG NIILGATVDT QLCDKLLTSS LQKSSSLGNL KKETSDGEKE
     TIQKTSEDRA PAESRPFGTL PPRPPGQDTS MDDNPFGTRK VRSSFGRGFF KIKSNKRTAS
     APNLAETEKE TAEHLDLAGA SSRPKDSQRN SPFQIPPPSP DSKKKSRGIM KLFGKLRRSQ
     STTFNPDDMS EPEFKRGGTR ATAGPRLGWS RDLGQSNSDL DMPFAKWTKE QVCNWLMEQG
     LGSYLNSGKH WIASGQTLLQ ASQQDLEKEL GIKHSLHRKK LQLALQALGS EEETNHGKLD
     FNWVTRWLDD IGLPQYKTQF DEGRVDGRML HYMTVDDLLS LKVVSVLHHL SIKRAIQVLR
     INNFEPNCLR RRPSDENTIA PSEVQKWTNH RVMEWLRSVD LAEYAPNLRG SGVHGGLMVL
     EPRFNVETMA QLLNIPPNKT LLRRHLATHF NLLIGAEAQH QKRDAMELPD YVLLTATAKV
     KPKKLAFSNF GNLRKKKQED GEEYVCPMEL GQASGSASKK GFKPGLDMRL YEEDDLDRLE
     QMEDSEGTVR QIGAFSEGIN NLTHMLKEDD MFKDFAARSP SASITDEDSN V
//