FBF1_HUMAN
ID FBF1_HUMAN Reviewed; 1133 AA.
AC Q8TES7; B5MEM5; Q96IF6; Q96JG4; Q96MA8;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Fas-binding factor 1;
DE Short=FBF-1;
DE AltName: Full=Protein albatross;
GN Name=FBF1; Synonyms=ALB, KIAA1863;
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 6), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH PARD3, AND VARIANTS VAL-65 AND GLY-151.
RC TISSUE=Lung;
RX PubMed=18838552; DOI=10.1083/jcb.200803133;
RA Sugimoto M., Inoko A., Shiromizu T., Nakayama M., Zou P., Yonemura S.,
RA Hayashi Y., Izawa I., Sasoh M., Uji Y., Kaibuchi K., Kiyono T., Inagaki M.;
RT "The keratin-binding protein Albatross regulates polarization of epithelial
RT cells.";
RL J. Cell Biol. 183:19-28(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 659-1133 (ISOFORM 2).
RC TISSUE=Spleen, and Testis;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-1133 (ISOFORM 4), AND VARIANT
RP GLY-151.
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 445-1133 (ISOFORM 1).
RC TISSUE=Muscle;
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 IDENTIFICATION.
RX PubMed=10978533; DOI=10.1016/s0167-4781(00)00163-9;
RA Schmidt T., Karsunky H., Frass B., Baum W., Denzel A., Moeroey T.;
RT "A novel protein (Fbf-1) that binds to CD95/APO-1/FAS and shows sequence
RT similarity to trichohyalin and plectin.";
RL Biochim. Biophys. Acta 1493:249-254(2000).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21399614; DOI=10.1038/emboj.2011.63;
RA Jakobsen L., Vanselow K., Skogs M., Toyoda Y., Lundberg E., Poser I.,
RA Falkenby L.G., Bennetzen M., Westendorf J., Nigg E.A., Uhlen M.,
RA Hyman A.A., Andersen J.S.;
RT "Novel asymmetrically localizing components of human centrosomes identified
RT by complementary proteomics methods.";
RL EMBO J. 30:1520-1535(2011).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23348840; DOI=10.1101/gad.207043.112;
RA Tanos B.E., Yang H.J., Soni R., Wang W.J., Macaluso F.P., Asara J.M.,
RA Tsou M.F.;
RT "Centriole distal appendages promote membrane docking, leading to cilia
RT initiation.";
RL Genes Dev. 27:163-168(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-960, 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 [12]
RP INTERACTION WITH TRAPPC14.
RX PubMed=31467083; DOI=10.1074/jbc.ra119.008615;
RA Cuenca A., Insinna C., Zhao H., John P., Weiss M.A., Lu Q., Walia V.,
RA Specht S., Manivannan S., Stauffer J., Peden A.A., Westlake C.J.;
RT "The C7orf43/TRAPPC14 component links the TRAPPII complex to Rabin8 for
RT preciliary vesicle tethering at the mother centriole during ciliogenesis.";
RL J. Biol. Chem. 294:15418-15434(2019).
CC -!- FUNCTION: Keratin-binding protein required for epithelial cell
CC polarization. Involved in apical junction complex (AJC) assembly via
CC its interaction with PARD3. Required for ciliogenesis.
CC {ECO:0000269|PubMed:18838552, ECO:0000269|PubMed:23348840}.
CC -!- SUBUNIT: May interact with FAS cytoplasmic domain (By similarity).
CC Interacts with PARD3 (By similarity) (PubMed:18838552). Interacts with
CC TRAPPC14 (PubMed:31467083). {ECO:0000250, ECO:0000269|PubMed:18838552,
CC ECO:0000269|PubMed:31467083}.
CC -!- INTERACTION:
CC Q8TES7-6; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-10244131, EBI-742038;
CC Q8TES7-6; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-10244131, EBI-2548012;
CC Q8TES7-6; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-10244131, EBI-739580;
CC Q8TES7-6; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-10244131, EBI-10171570;
CC Q8TES7-6; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-10244131, EBI-747776;
CC Q8TES7-6; Q96MT8: CEP63; NbExp=3; IntAct=EBI-10244131, EBI-741977;
CC Q8TES7-6; Q9BW66: CINP; NbExp=3; IntAct=EBI-10244131, EBI-739784;
CC Q8TES7-6; Q05D60: DEUP1; NbExp=6; IntAct=EBI-10244131, EBI-748597;
CC Q8TES7-6; P15976: GATA1; NbExp=3; IntAct=EBI-10244131, EBI-3909284;
CC Q8TES7-6; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10244131, EBI-618309;
CC Q8TES7-6; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-10244131, EBI-747204;
CC Q8TES7-6; A1A4E9: KRT13; NbExp=3; IntAct=EBI-10244131, EBI-10171552;
CC Q8TES7-6; Q15323: KRT31; NbExp=3; IntAct=EBI-10244131, EBI-948001;
CC Q8TES7-6; Q6A162: KRT40; NbExp=3; IntAct=EBI-10244131, EBI-10171697;
CC Q8TES7-6; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-10244131, EBI-741037;
CC Q8TES7-6; P50222: MEOX2; NbExp=3; IntAct=EBI-10244131, EBI-748397;
CC Q8TES7-6; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-10244131, EBI-10172526;
CC Q8TES7-6; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-10244131, EBI-2548751;
CC Q8TES7-6; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-10244131, EBI-302345;
CC Q8TES7-6; Q93062: RBPMS; NbExp=3; IntAct=EBI-10244131, EBI-740322;
CC Q8TES7-6; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-10244131, EBI-2212028;
CC Q8TES7-6; P63165: SUMO1; NbExp=3; IntAct=EBI-10244131, EBI-80140;
CC Q8TES7-6; O75478: TADA2A; NbExp=3; IntAct=EBI-10244131, EBI-742268;
CC Q8TES7-6; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-10244131, EBI-10172380;
CC Q8TES7-6; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-10244131, EBI-742397;
CC Q8TES7-6; Q08117: TLE5; NbExp=3; IntAct=EBI-10244131, EBI-717810;
CC Q8TES7-6; Q13077: TRAF1; NbExp=3; IntAct=EBI-10244131, EBI-359224;
CC Q8TES7-6; P36406: TRIM23; NbExp=3; IntAct=EBI-10244131, EBI-740098;
CC Q8TES7-6; P14373: TRIM27; NbExp=3; IntAct=EBI-10244131, EBI-719493;
CC Q8TES7-6; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-10244131, EBI-2130429;
CC Q8TES7-6; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-10244131, EBI-744794;
CC Q8TES7-6; Q5I0X7: TTC32; NbExp=3; IntAct=EBI-10244131, EBI-8636434;
CC Q8TES7-6; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10244131, EBI-739895;
CC Q8TES7-6; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-10244131, EBI-4400866;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole. Cytoplasm, cytoskeleton, spindle pole.
CC Cell junction. Note=Localizes specifically to the distal appendage
CC region of the centriole, which anchors the mother centriole to the
CC plasma membrane. Localizes to the apical junction complex (AJC) in
CC epithelial cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8TES7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TES7-2; Sequence=VSP_027322, VSP_027323;
CC Name=3;
CC IsoId=Q8TES7-3; Sequence=VSP_027320, VSP_027321;
CC Name=4;
CC IsoId=Q8TES7-4; Sequence=VSP_027318, VSP_027319;
CC Name=5;
CC IsoId=Q8TES7-5; Sequence=VSP_040769, VSP_040770;
CC Name=6;
CC IsoId=Q8TES7-6; Sequence=VSP_041555, VSP_040770;
CC -!- TISSUE SPECIFICITY: Present in various epithelial cells (at protein
CC level).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71400.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB84871.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB354594; BAG71501.1; -; mRNA.
DR EMBL; AK057261; BAB71400.1; ALT_INIT; mRNA.
DR EMBL; AK074045; BAB84871.1; ALT_INIT; mRNA.
DR EMBL; AC087289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB058766; BAB47492.1; -; mRNA.
DR EMBL; BC007570; AAH07570.1; -; mRNA.
DR CCDS; CCDS45779.2; -. [Q8TES7-6]
DR RefSeq; NP_001306122.1; NM_001319193.1. [Q8TES7-6]
DR AlphaFoldDB; Q8TES7; -.
DR SMR; Q8TES7; -.
DR BioGRID; 124465; 165.
DR IntAct; Q8TES7; 139.
DR MINT; Q8TES7; -.
DR STRING; 9606.ENSP00000324292; -.
DR GlyGen; Q8TES7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TES7; -.
DR PhosphoSitePlus; Q8TES7; -.
DR BioMuta; FBF1; -.
DR DMDM; 156630449; -.
DR EPD; Q8TES7; -.
DR jPOST; Q8TES7; -.
DR MassIVE; Q8TES7; -.
DR MaxQB; Q8TES7; -.
DR PaxDb; Q8TES7; -.
DR PeptideAtlas; Q8TES7; -.
DR PRIDE; Q8TES7; -.
DR ProteomicsDB; 74489; -. [Q8TES7-1]
DR ProteomicsDB; 74490; -. [Q8TES7-2]
DR ProteomicsDB; 74491; -. [Q8TES7-3]
DR ProteomicsDB; 74492; -. [Q8TES7-4]
DR ProteomicsDB; 74493; -. [Q8TES7-5]
DR ProteomicsDB; 74494; -. [Q8TES7-6]
DR Antibodypedia; 80115; 93 antibodies from 21 providers.
DR DNASU; 85302; -.
DR Ensembl; ENST00000586717.5; ENSP00000465132.1; ENSG00000188878.20. [Q8TES7-1]
DR Ensembl; ENST00000636174.2; ENSP00000490726.1; ENSG00000188878.20. [Q8TES7-6]
DR GeneID; 85302; -.
DR KEGG; hsa:85302; -.
DR MANE-Select; ENST00000636174.2; ENSP00000490726.1; NM_001319193.2; NP_001306122.1. [Q8TES7-6]
DR UCSC; uc002jqd.2; human. [Q8TES7-1]
DR CTD; 85302; -.
DR DisGeNET; 85302; -.
DR GeneCards; FBF1; -.
DR HGNC; HGNC:24674; FBF1.
DR HPA; ENSG00000188878; Tissue enhanced (testis).
DR neXtProt; NX_Q8TES7; -.
DR OpenTargets; ENSG00000188878; -.
DR VEuPathDB; HostDB:ENSG00000188878; -.
DR eggNOG; ENOG502QQFR; Eukaryota.
DR GeneTree; ENSGT00720000108861; -.
DR InParanoid; Q8TES7; -.
DR OMA; DKEDPWG; -.
DR OrthoDB; 399859at2759; -.
DR PhylomeDB; Q8TES7; -.
DR TreeFam; TF328742; -.
DR PathwayCommons; Q8TES7; -.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR SignaLink; Q8TES7; -.
DR BioGRID-ORCS; 85302; 9 hits in 1072 CRISPR screens.
DR GenomeRNAi; 85302; -.
DR Pharos; Q8TES7; Tbio.
DR PRO; PR:Q8TES7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8TES7; protein.
DR Bgee; ENSG00000188878; Expressed in right testis and 93 other tissues.
DR ExpressionAtlas; Q8TES7; baseline and differential.
DR Genevisible; Q8TES7; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0097539; C:ciliary transition fiber; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0043297; P:apical junction assembly; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IMP:UniProtKB.
DR InterPro; IPR033561; FBF1.
DR PANTHER; PTHR33689; PTHR33689; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1133
FT /note="Fas-binding factor 1"
FT /id="PRO_0000297646"
FT REGION 89..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 577..727
FT /evidence="ECO:0000255"
FT COILED 773..870
FT /evidence="ECO:0000255"
FT COMPBIAS 162..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..393
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 960
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 11
FT /note="V -> GSIDDFLGDLLGDDM (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:18838552"
FT /id="VSP_041555"
FT VAR_SEQ 309
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_040769"
FT VAR_SEQ 462..517
FT /note="QPLTSTQGLEHAAAGGSSGTTARERPCVRPGVSGSPVTQNHAASALPTGSPK
FT RGTA -> LTWAFCHLHLERCLSSANLSPAHKGLSTQLLEGVLEQLHEKDRVSGLVSRG
FT PL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11347906"
FT /id="VSP_027318"
FT VAR_SEQ 518..1133
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11347906"
FT /id="VSP_027319"
FT VAR_SEQ 599..662
FT /note="KLELERAQHELLLGSLQQQHQADLELIESAHRSRIKVLETSYQQREERLRRE
FT NEELSARYLSQC -> GSGAVGAGGRVATGGDTESGWKLPQEGGRAVGTGQRGVQPPPL
FT PGCWPSCCLPGAEAGARTGPA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027320"
FT VAR_SEQ 663..1133
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027321"
FT VAR_SEQ 897..899
FT /note="SKE -> RAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027322"
FT VAR_SEQ 900..1133
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027323"
FT VAR_SEQ 924
FT /note="K -> KE (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:18838552"
FT /id="VSP_040770"
FT VARIANT 65
FT /note="G -> V (in dbSNP:rs1135889)"
FT /evidence="ECO:0000269|PubMed:18838552"
FT /id="VAR_034659"
FT VARIANT 151
FT /note="R -> G (in dbSNP:rs2305913)"
FT /evidence="ECO:0000269|PubMed:11347906,
FT ECO:0000269|PubMed:18838552"
FT /id="VAR_034660"
FT VARIANT 371
FT /note="P -> S (in dbSNP:rs7218738)"
FT /id="VAR_034661"
FT VARIANT 574
FT /note="C -> S (in dbSNP:rs7213548)"
FT /id="VAR_034662"
FT CONFLICT 801
FT /note="Q -> R (in Ref. 2; BAB71400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1133 AA; 125446 MW; 58FA2446CBA3C6B7 CRC64;
MAPKTKKGCK VTLPEKPVKL ASHTRDTTGV SQMFPSSKAR TKSLLGDDVF STMAGLEEAD
AEVSGISEAD PQALLQAMKD LDGMDADILG LKKSNSAPSK KAAKDPGKGE LPNHPKPAGG
AIPTKKSLPS PSSSGHQNRR FSSEDLEDPL RGLLSYDEGG ITKQPPVTQS KTASDKSPST
VRDQGPSIPL TPGDTPIRKK EELLFDDGDD IMATLGFGDS PKAEKRQIGD QEGPRPARST
LDELLGRGMA TKLLARPGTG EHREFKLDKK YQRPQDSEDM WGDEDFTFGA YQPTVVSSEG
RQSRRQSVSR FFADSGADPK GEPGSKQSPP MASSPIQPRK GGADWLGLKD EDLDLFPASP
TREAHRESSV PVTPSVPPPA SQHSTPAGLP PSRAKPPTEG AGSPAKASQA SKLRASKEEK
EDWLSHALSR KKSQGLAREQ HAGTSEGLHL AGTAGHPPSG SQPLTSTQGL EHAAAGGSSG
TTARERPCVR PGVSGSPVTQ NHAASALPTG SPKRGTAPGD LSATEPATCF PSTQKPTEPS
VPVQPLLPES LARSLLPSTE YQKQLLAAQV QLQCSPAELQ AELLHSQARL AELEAQVRKL
ELERAQHELL LGSLQQQHQA DLELIESAHR SRIKVLETSY QQREERLRRE NEELSARYLS
QCQEAEQARA ELTAQHQRRL AAIAQEKDQE MERLRELQRA SILDMRRDHE EQLQRLKLLK
DREVDAATSA TSHTRSLNSI IHQMEKFSSS LHELSSRVEA SHLTTSQERE LGIRQRDEQL
RALQERLGQQ QRDMEEERSR QQEVIGKMEA RLNEQSRLLE QERWRVTAEQ SKAESMQRAL
EEQRKVTAQQ MAMERAELER AKSALLEEQK SVMLKCGEER RRLAAEWAEF SAQQKLSKER
AEREAERALQ VDTQREGTLI SLAKQAELKI RASELRAEEK QLAAERAALE QERQELRLEK
ERINATALRV KLRAEEVESM SKVASEKYEE GERALREAQQ VQAEQQARLQ AVQQQQERLR
KQEQHMHQEH LSLAQQRLQL DRARQDLPSS LVGLFPRAQG PAASSQSALM PPAPTTRWCS
QPPTGLDPSP LHLHARLALL RHMAEQDRDF LENEQFFLET LKKGSYNLTS HSA
