TCOF_HUMAN
ID TCOF_HUMAN Reviewed; 1488 AA.
AC Q13428; A0JLU0; B4E111; Q6SC72; Q7Z5W9; Q96A52; Q99408; Q99860;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Treacle protein;
DE AltName: Full=Treacher Collins syndrome protein;
GN Name=TCOF1;
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), AND VARIANTS PRO-665 AND ALA-887.
RX PubMed=8563749; DOI=10.1038/ng0296-130;
RA Dixon J., Edwards S.J., Gladwin A.J., Dixon M.J., Loftus S.K., Bonner C.A.,
RA Koprivnikar K., Wasmuth J.J.;
RT "Positional cloning of a gene involved in the pathogenesis of Treacher
RT Collins syndrome.";
RL Nat. Genet. 12:130-136(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND VARIANTS PRO-665
RP AND ALA-887.
RX PubMed=9074926; DOI=10.1101/gr.7.3.223;
RA Dixon J., Edwards S.J., Anderson I., Brass A., Scambler P.J., Dixon M.J.;
RT "Identification of the complete coding sequence and genomic organization of
RT the Treacher Collins syndrome gene.";
RL Genome Res. 7:223-234(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS PRO-665 AND ALA-887.
RX PubMed=9096354; DOI=10.1073/pnas.94.7.3110;
RA Wise C.A., Chiang L.C., Paznekas W.A., Sharma M., Musy M.M., Ashley J.A.,
RA Lovett M., Jabs E.W.;
RT "TCOF1 gene encodes a putative nucleolar phosphoprotein that exhibits
RT mutations in Treacher Collins syndrome throughout its coding region.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3110-3115(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 4),
RP AND VARIANTS PRO-665 AND ALA-887.
RX PubMed=15019983; DOI=10.1016/j.gene.2003.11.027;
RA So R.B., Gonzales B., Henning D., Dixon J., Dixon M.J., Valdez B.C.;
RT "Another face of the Treacher Collins syndrome (TCOF1) gene: identification
RT of additional exons.";
RL Gene 328:49-57(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1448 (ISOFORM 6), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 16-1188 (ISOFORM 3).
RC TISSUE=Eye, 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1452 (ISOFORM 7), AND VARIANT
RP ALA-887.
RC TISSUE=Thymus;
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 [8]
RP PROTEIN SEQUENCE OF 63-74; 101-122; 135-155; 297-308; 368-379; 433-444;
RP 503-519; 571-586; 706-716; 733-755; 792-803; 893-904; 1065-1078; 1130-1138;
RP 1225-1238; 1245-1259; 1318-1329 AND 1424-1437, FUNCTION, SUBCELLULAR
RP LOCATION, IDENTIFICATION IN A PRE-RIBOSOMAL RNP COMPLEX, INTERACTION WITH
RP NOP56, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12777385; DOI=10.1074/jbc.m304304200;
RA Hayano T., Yanagida M., Yamauchi Y., Shinkawa T., Isobe T., Takahashi N.;
RT "Proteomic analysis of human Nop56p-associated pre-ribosomal
RT ribonucleoprotein complexes. Possible link between Nop56p and the nucleolar
RT protein treacle responsible for Treacher Collins syndrome.";
RL J. Biol. Chem. 278:34309-34319(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-446; SER-620;
RP SER-906; SER-1257 AND SER-1350, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-249; SER-1111; SER-1228 AND
RP SER-1378, AND IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-446; SER-906 AND
RP THR-914, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906 AND SER-967, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906 AND SER-1350, AND
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; THR-84; SER-85; SER-87;
RP SER-88; SER-153; SER-156; THR-310; THR-316; SER-381; SER-503; THR-581;
RP SER-583; SER-762; SER-764; SER-765; SER-769; SER-771; SER-777; SER-868;
RP SER-870; SER-871; SER-875; SER-877; SER-998; SER-1111; SER-1190; SER-1228;
RP THR-1234; SER-1257; SER-1376; SER-1378; SER-1407 AND SER-1410, AND
RP IDENTIFICATION BY MASS 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 [16]
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; THR-249; SER-381;
RP SER-583; THR-983; SER-1111; SER-1228; SER-1376 AND SER-1378, 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-155; LYS-296; LYS-600; LYS-755
RP AND LYS-1414, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-233; THR-249;
RP THR-310; SER-381; SER-446; SER-503; SER-583; SER-868; SER-870; SER-871;
RP SER-875; SER-877; SER-906; THR-914; SER-1257; SER-1350; SER-1378 AND
RP SER-1410, 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 [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-233; SER-381;
RP SER-446; SER-503; SER-583; SER-906; SER-967; SER-1228; SER-1350; SER-1376
RP AND SER-1378, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-156; THR-249;
RP SER-381; SER-484; SER-503; THR-533; THR-581; SER-583; SER-906; THR-914;
RP THR-983; THR-1175; SER-1228; SER-1257; SER-1350; THR-1358; SER-1376;
RP SER-1378; SER-1407 AND SER-1410, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-381; SER-1228;
RP SER-1257 AND SER-1350, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-600; LYS-755 AND LYS-1414, 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 [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-755, AND IDENTIFICATION BY MASS
RP 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 [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-126; LYS-755 AND LYS-1414, AND
RP IDENTIFICATION BY MASS 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 [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-600 AND LYS-755, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [29]
RP FUNCTION, UBIQUITINATION, AND SUBUNIT.
RX PubMed=26399832; DOI=10.1038/nature14978;
RA Werner A., Iwasaki S., McGourty C.A., Medina-Ruiz S., Teerikorpi N.,
RA Fedrigo I., Ingolia N.T., Rape M.;
RT "Cell-fate determination by ubiquitin-dependent regulation of
RT translation.";
RL Nature 525:523-527(2015).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-507; LYS-600; LYS-637; LYS-725;
RP LYS-732; LYS-755; LYS-1224; LYS-1238; LYS-1248 AND LYS-1414, 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 [31]
RP VARIANTS LEU-516; ALA-887; VAL-1390 AND GLY-1432, AND VARIANT TCS1 ARG-53.
RX PubMed=9042910;
RA Edwards S.J., Gladwin A.J., Dixon M.J.;
RT "The mutational spectrum in Treacher Collins syndrome reveals a
RT predominance of mutations that create a premature-termination codon.";
RL Am. J. Hum. Genet. 60:515-524(1997).
RN [32]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-1030.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Nucleolar protein that acts as a regulator of RNA polymerase
CC I by connecting RNA polymerase I with enzymes responsible for ribosomal
CC processing and modification (PubMed:12777385, PubMed:26399832).
CC Required for neural crest specification: following monoubiquitination
CC by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a
CC platform to connect RNA polymerase I with enzymes responsible for
CC ribosomal processing and modification, leading to remodel the
CC translational program of differentiating cells in favor of neural crest
CC specification (PubMed:26399832). {ECO:0000269|PubMed:12777385,
CC ECO:0000269|PubMed:26399832}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with NOLC1 following
CC monoubiquitination (PubMed:26399832). Part of a large pre-ribosomal
CC ribonucleoprotein (RNP) complex, that consists of at least 62 ribosomal
CC proteins, 45 nonribosomal proteins and both pre-rRNA and mature rRNA
CC species. Within this complex directly interacts with NOP56 in an RNA-
CC independent manner (PubMed:12777385). {ECO:0000269|PubMed:12777385,
CC ECO:0000269|PubMed:26399832}.
CC -!- INTERACTION:
CC Q13428; P49407: ARRB1; NbExp=3; IntAct=EBI-396105, EBI-743313;
CC Q13428; P32121: ARRB2; NbExp=3; IntAct=EBI-396105, EBI-714559;
CC Q13428; O60934: NBN; NbExp=10; IntAct=EBI-396105, EBI-494844;
CC Q13428; P78362: SRPK2; NbExp=2; IntAct=EBI-396105, EBI-593303;
CC Q13428-5; Q06481-5: APLP2; NbExp=3; IntAct=EBI-25832010, EBI-25646567;
CC Q13428-5; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-25832010, EBI-1055945;
CC Q13428-5; P16284: PECAM1; NbExp=3; IntAct=EBI-25832010, EBI-716404;
CC Q13428-5; P37173: TGFBR2; NbExp=3; IntAct=EBI-25832010, EBI-296151;
CC Q13428-5; P08670: VIM; NbExp=3; IntAct=EBI-25832010, EBI-353844;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12777385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q13428-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13428-2; Sequence=VSP_022295;
CC Name=3;
CC IsoId=Q13428-3; Sequence=VSP_022297;
CC Name=4;
CC IsoId=Q13428-4; Sequence=VSP_022296;
CC Name=5;
CC IsoId=Q13428-5; Sequence=VSP_023133, VSP_023134;
CC Name=6;
CC IsoId=Q13428-6; Sequence=VSP_040382;
CC Name=7;
CC IsoId=Q13428-7; Sequence=VSP_040382, VSP_022297;
CC Name=8;
CC IsoId=Q13428-8; Sequence=VSP_022295, VSP_022297;
CC -!- PTM: Ubiquitinated. Monoubiquitination by the BCR(KBTBD8) complex
CC promotes the formation of a NOLC1-TCOF1 complex that acts as a platform
CC to connect RNA polymerase I with enzymes responsible for ribosomal
CC processing and modification, leading to remodel the translational
CC program of differentiating cells in favor of neural crest specification
CC (PubMed:26399832). {ECO:0000269|PubMed:26399832}.
CC -!- PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-
CC IP7). Serine pyrophosphorylation is achieved by Mg(2+)-dependent, but
CC enzyme independent transfer of a beta-phosphate from a inositol
CC pyrophosphate to a pre-phosphorylated serine residue.
CC {ECO:0000250|UniProtKB:O08784}.
CC -!- DISEASE: Treacher Collins syndrome 1 (TCS1) [MIM:154500]: A form of
CC Treacher Collins syndrome, a disorder of craniofacial development.
CC Treacher Collins syndrome is characterized by a combination of
CC bilateral downward slanting of the palpebral fissures, colobomas of the
CC lower eyelids with a paucity of eyelashes medial to the defect,
CC hypoplasia of the facial bones, cleft palate, malformation of the
CC external ears, atresia of the external auditory canals, and bilateral
CC conductive hearing loss. {ECO:0000269|PubMed:9042910}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 1]: Major.
CC -!- MISCELLANEOUS: [Isoform 4]: Minor. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16144.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; U40847; AAC50903.1; -; mRNA.
DR EMBL; U76366; AAC51181.1; -; mRNA.
DR EMBL; U84664; AAC51185.1; -; Genomic_DNA.
DR EMBL; U84640; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84641; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84642; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84643; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84644; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84645; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84646; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84647; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84648; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84649; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84650; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84651; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84652; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84653; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84654; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84655; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84656; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84657; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84658; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84659; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84660; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84661; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84662; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U84663; AAC51185.1; JOINED; Genomic_DNA.
DR EMBL; U79659; AAB40722.1; -; Genomic_DNA.
DR EMBL; U79645; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79646; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79647; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79648; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79649; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79650; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79651; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79652; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79653; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79654; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79655; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79656; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79657; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; U79658; AAB40722.1; JOINED; Genomic_DNA.
DR EMBL; AY460334; AAR87774.1; -; mRNA.
DR EMBL; AC011372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011764; AAH11764.1; -; mRNA.
DR EMBL; BC014559; AAH14559.1; -; mRNA.
DR EMBL; BC016144; AAH16144.1; ALT_SEQ; mRNA.
DR EMBL; BC027252; AAH27252.1; -; mRNA.
DR EMBL; BC033093; AAH33093.1; -; mRNA.
DR EMBL; AK303611; BAG64623.1; -; mRNA.
DR CCDS; CCDS4306.1; -. [Q13428-2]
DR CCDS; CCDS47305.1; -. [Q13428-7]
DR CCDS; CCDS47306.1; -. [Q13428-8]
DR CCDS; CCDS47307.1; -. [Q13428-5]
DR CCDS; CCDS54936.1; -. [Q13428-1]
DR RefSeq; NP_000347.2; NM_000356.3. [Q13428-2]
DR RefSeq; NP_001008657.1; NM_001008657.2. [Q13428-5]
DR RefSeq; NP_001128715.1; NM_001135243.1. [Q13428-1]
DR RefSeq; NP_001128716.1; NM_001135244.1. [Q13428-7]
DR RefSeq; NP_001128717.1; NM_001135245.1. [Q13428-8]
DR RefSeq; NP_001182070.1; NM_001195141.1. [Q13428-6]
DR RefSeq; XP_005268562.1; XM_005268505.3.
DR AlphaFoldDB; Q13428; -.
DR SMR; Q13428; -.
DR BioGRID; 112809; 198.
DR CORUM; Q13428; -.
DR DIP; DIP-32953N; -.
DR IntAct; Q13428; 64.
DR MINT; Q13428; -.
DR STRING; 9606.ENSP00000367028; -.
DR GlyGen; Q13428; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q13428; -.
DR MetOSite; Q13428; -.
DR PhosphoSitePlus; Q13428; -.
DR SwissPalm; Q13428; -.
DR BioMuta; TCOF1; -.
DR DMDM; 302393806; -.
DR EPD; Q13428; -.
DR jPOST; Q13428; -.
DR MassIVE; Q13428; -.
DR MaxQB; Q13428; -.
DR PaxDb; Q13428; -.
DR PeptideAtlas; Q13428; -.
DR PRIDE; Q13428; -.
DR ProteomicsDB; 59417; -. [Q13428-1]
DR ProteomicsDB; 59418; -. [Q13428-2]
DR ProteomicsDB; 59419; -. [Q13428-3]
DR ProteomicsDB; 59420; -. [Q13428-4]
DR ProteomicsDB; 59421; -. [Q13428-5]
DR ProteomicsDB; 59422; -. [Q13428-6]
DR ProteomicsDB; 59423; -. [Q13428-7]
DR ProteomicsDB; 59424; -. [Q13428-8]
DR TopDownProteomics; Q13428-5; -. [Q13428-5]
DR Antibodypedia; 27956; 199 antibodies from 30 providers.
DR DNASU; 6949; -.
DR Ensembl; ENST00000323668.11; ENSP00000325223.6; ENSG00000070814.22. [Q13428-2]
DR Ensembl; ENST00000377797.7; ENSP00000367028.4; ENSG00000070814.22. [Q13428-1]
DR Ensembl; ENST00000394269.7; ENSP00000377811.3; ENSG00000070814.22. [Q13428-5]
DR Ensembl; ENST00000427724.7; ENSP00000390717.3; ENSG00000070814.22. [Q13428-6]
DR Ensembl; ENST00000439160.6; ENSP00000406888.2; ENSG00000070814.22. [Q13428-7]
DR Ensembl; ENST00000445265.6; ENSP00000409944.2; ENSG00000070814.22. [Q13428-8]
DR Ensembl; ENST00000504761.6; ENSP00000421655.2; ENSG00000070814.22. [Q13428-1]
DR Ensembl; ENST00000643257.2; ENSP00000493815.1; ENSG00000070814.22. [Q13428-3]
DR GeneID; 6949; -.
DR KEGG; hsa:6949; -.
DR MANE-Select; ENST00000643257.2; ENSP00000493815.1; NM_001371623.1; NP_001358552.1. [Q13428-3]
DR UCSC; uc003lrw.4; human. [Q13428-1]
DR CTD; 6949; -.
DR DisGeNET; 6949; -.
DR GeneCards; TCOF1; -.
DR GeneReviews; TCOF1; -.
DR HGNC; HGNC:11654; TCOF1.
DR HPA; ENSG00000070814; Tissue enhanced (brain).
DR MalaCards; TCOF1; -.
DR MIM; 154500; phenotype.
DR MIM; 606847; gene.
DR neXtProt; NX_Q13428; -.
DR OpenTargets; ENSG00000070814; -.
DR Orphanet; 861; Treacher-Collins syndrome.
DR PharmGKB; PA36405; -.
DR VEuPathDB; HostDB:ENSG00000070814; -.
DR eggNOG; ENOG502S41N; Eukaryota.
DR GeneTree; ENSGT00730000111382; -.
DR HOGENOM; CLU_263315_0_0_1; -.
DR InParanoid; Q13428; -.
DR OMA; VYDTPRN; -.
DR OrthoDB; 614008at2759; -.
DR PhylomeDB; Q13428; -.
DR TreeFam; TF341730; -.
DR PathwayCommons; Q13428; -.
DR SignaLink; Q13428; -.
DR SIGNOR; Q13428; -.
DR BioGRID-ORCS; 6949; 506 hits in 1082 CRISPR screens.
DR ChiTaRS; TCOF1; human.
DR GeneWiki; Treacle_protein; -.
DR GenomeRNAi; 6949; -.
DR Pharos; Q13428; Tbio.
DR PRO; PR:Q13428; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q13428; protein.
DR Bgee; ENSG00000070814; Expressed in sural nerve and 196 other tissues.
DR ExpressionAtlas; Q13428; baseline and differential.
DR Genevisible; Q13428; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:CAFA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:CAFA.
DR GO; GO:0014032; P:neural crest cell development; IMP:UniProtKB.
DR GO; GO:0014029; P:neural crest formation; IMP:UniProtKB.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IMP:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR017859; Treacle.
DR InterPro; IPR003993; Treacle_dom.
DR PANTHER; PTHR20787; PTHR20787; 2.
DR Pfam; PF03546; Treacle; 4.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW Disease variant; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1488
FT /note="Treacle protein"
FT /id="PRO_0000072459"
FT DOMAIN 6..38
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 57..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1462
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1488
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 134
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 155
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 249
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 296
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 310
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 313
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 322
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 533
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 581
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 600
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 716
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 720
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 755
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 870
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 914
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 974
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 983
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"
FT MOD_RES 1175
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 1228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1358
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1378
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 1407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1414
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT MOD_RES 1471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08784"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364"
FT CROSSLNK 507
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 600
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:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 637
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 725
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 732
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 755
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 755
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:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1414
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:25772364, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 214..290
FT /note="Missing (in isoform 2 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:8563749,
FT ECO:0000303|PubMed:9074926"
FT /id="VSP_022295"
FT VAR_SEQ 953
FT /note="Q -> QDSNSKPARSKTLAPAPPERNTEGSSESSEEELPLTQ (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_022296"
FT VAR_SEQ 954..958
FT /note="VIKPP -> DQESS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023133"
FT VAR_SEQ 959..1488
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023134"
FT VAR_SEQ 1062..1099
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_040382"
FT VAR_SEQ 1172
FT /note="L -> LV (in isoform 3, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022297"
FT VARIANT 53
FT /note="W -> R (in TCS1)"
FT /evidence="ECO:0000269|PubMed:9042910"
FT /id="VAR_005630"
FT VARIANT 221
FT /note="A -> P (in dbSNP:rs11541811)"
FT /id="VAR_057002"
FT VARIANT 516
FT /note="P -> L (in dbSNP:rs138645438)"
FT /evidence="ECO:0000269|PubMed:9042910"
FT /id="VAR_005631"
FT VARIANT 665
FT /note="A -> P (in dbSNP:rs2071240)"
FT /evidence="ECO:0000269|PubMed:15019983,
FT ECO:0000269|PubMed:8563749, ECO:0000269|PubMed:9074926,
FT ECO:0000269|PubMed:9096354"
FT /id="VAR_029869"
FT VARIANT 887
FT /note="V -> A (in dbSNP:rs7713638)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15019983, ECO:0000269|PubMed:8563749,
FT ECO:0000269|PubMed:9042910, ECO:0000269|PubMed:9074926,
FT ECO:0000269|PubMed:9096354"
FT /id="VAR_005632"
FT VARIANT 1030
FT /note="R -> K (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1206146416)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035666"
FT VARIANT 1176
FT /note="P -> R (in dbSNP:rs1136103)"
FT /id="VAR_059729"
FT VARIANT 1280
FT /note="G -> R (in dbSNP:rs11541812)"
FT /id="VAR_059730"
FT VARIANT 1390
FT /note="A -> V (in dbSNP:rs15251)"
FT /evidence="ECO:0000269|PubMed:9042910"
FT /id="VAR_005633"
FT VARIANT 1431
FT /note="G -> A (in dbSNP:rs45491898)"
FT /id="VAR_061709"
FT VARIANT 1432
FT /note="D -> G (in dbSNP:rs151344580)"
FT /evidence="ECO:0000269|PubMed:9042910"
FT /id="VAR_005634"
FT CONFLICT 1271
FT /note="P -> L (in Ref. 7; BAG64623)"
FT /evidence="ECO:0000305"
FT CONFLICT 1389
FT /note="K -> Q (in Ref. 2; AAB40722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1488 AA; 152106 MW; 6348306D0479790B CRC64;
MAEARKRREL LPLIYHHLLR AGYVRAAREV KEQSGQKCFL AQPVTLLDIY THWQQTSELG
RKRKAEEDAA LQAKKTRVSD PISTSESSEE EEEAEAETAK ATPRLASTNS SVLGADLPSS
MKEKAKAETE KAGKTGNSMP HPATGKTVAN LLSGKSPRKS AEPSANTTLV SETEEEGSVP
AFGAAAKPGM VSAGQADSSS EDTSSSSDET DVEGKPSVKP AQVKASSVST KESPARKAAP
APGKVGDVTP QVKGGALPPA KRAKKPEEES ESSEEGSESE EEAPAGTRSQ VKASEKILQV
RAASAPAKGT PGKGATPAPP GKAGAVASQT KAGKPEEDSE SSSEESSDSE EETPAAKALL
QAKASGKTSQ VGAASAPAKE SPRKGAAPAP PGKTGPAVAK AQAGKREEDS QSSSEESDSE
EEAPAQAKPS GKAPQVRAAS APAKESPRKG AAPAPPRKTG PAAAQVQVGK QEEDSRSSSE
ESDSDREALA AMNAAQVKPL GKSPQVKPAS TMGMGPLGKG AGPVPPGKVG PATPSAQVGK
WEEDSESSSE ESSDSSDGEV PTAVAPAQEK SLGNILQAKP TSSPAKGPPQ KAGPVAVQVK
AEKPMDNSES SEESSDSADS EEAPAAMTAA QAKPALKIPQ TKACPKKTNT TASAKVAPVR
VGTQAPRKAG TATSPAGSSP AVAGGTQRPA EDSSSSEESD SEEEKTGLAV TVGQAKSVGK
GLQVKAASVP VKGSLGQGTA PVLPGKTGPT VTQVKAEKQE DSESSEEESD SEEAAASPAQ
VKTSVKKTQA KANPAAARAP SAKGTISAPG KVVTAAAQAK QRSPSKVKPP VRNPQNSTVL
ARGPASVPSV GKAVATAAQA QTGPEEDSGS SEEESDSEEE AETLAQVKPS GKTHQIRAAL
APAKESPRKG AAPTPPGKTG PSAAQAGKQD DSGSSSEESD SDGEAPAAVT SAQVIKPPLI
FVDPNRSPAG PAATPAQAQA ASTPRKARAS ESTARSSSSE SEDEDVIPAT QCLTPGIRTN
VVTMPTAHPR IAPKASMAGA SSSKESSRIS DGKKQEGPAT QVSKKNPASL PLTQAALKVL
AQKASEAQPP VARTQPSSGV DSAVGTLPAT SPQSTSVQAK GTNKLRKPKL PEVQQATKAP
ESSDDSEDSS DSSSGSEEDG EGPQGAKSAH TLGPTPSRTE TLVEETAAES SEDDVVAPSQ
SLLSGYMTPG LTPANSQASK ATPKLDSSPS VSSTLAAKDD PDGKQEAKPQ QAAGMLSPKT
GGKEAASGTT PQKSRKPKKG AGNPQASTLA LQSNITQCLL GQPWPLNEAQ VQASVVKVLT
ELLEQERKKV VDTTKESSRK GWESRKRKLS GDQPAARTPR SKKKKKLGAG EGGEASVSPE
KTSTTSKGKA KRDKASGDVK EKKGKGSLGS QGAKDEPEEE LQKGMGTVEG GDQSNPKSKK
EKKKSDKRKK DKEKKEKKKK AKKASTKDSE SPSQKKKKKK KKTAEQTV
