ID BCLF1_HUMAN Reviewed; 920 AA. AC Q9NYF8; A2RU75; B7ZM58; E1P586; Q14673; Q86WU6; Q86WY0; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 2. DT 27-MAR-2024, entry version 200. DE RecName: Full=Bcl-2-associated transcription factor 1; DE Short=Btf; DE AltName: Full=BCLAF1 and THRAP3 family member 1; GN Name=BCLAF1; Synonyms=BTF, KIAA0164; 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] (ISOFORMS 2 AND 3). RX PubMed=10330179; DOI=10.1128/mcb.19.6.4390; RA Kasof G.M., Goyal L., White E.; RT "Btf, a novel death-promoting transcriptional repressor that interacts with RT Bcl-2-related proteins."; RL Mol. Cell. Biol. 19:4390-4404(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=8724849; DOI=10.1093/dnares/3.1.17; RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. V. The RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 3:17-24(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-676 (ISOFORM 4). RC TISSUE=Brain, Pancreas, Testis, and Uterus; 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 PROTEIN SEQUENCE OF 168-182; 189-204; 256-271; 284-298; 304-312; 319-332; RP 394-409; 422-439; 461-475; 505-517; 525-534; 537-548; 551-581; 587-593; RP 623-631; 654-664; 785-796; 832-842 AND 846-852, PHOSPHORYLATION AT SER-177; RP SER-268; SER-290; SER-512; SER-531 AND SER-658, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Colon carcinoma; RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.; RL Submitted (APR-2008) to UniProtKB. RN [7] RP INTERACTION WITH EMD. RX PubMed=15009215; DOI=10.1111/j.1432-1033.2004.04007.x; RA Haraguchi T., Holaska J.M., Yamane M., Koujin T., Hashiguchi N., Mori C., RA Wilson K.L., Hiraoka Y.; RT "Emerin binding to Btf, a death-promoting transcriptional repressor, is RT disrupted by a missense mutation that causes Emery-Dreifuss muscular RT dystrophy."; RL Eur. J. Biochem. 271:1035-1045(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-389; SER-397; RP THR-402; SER-531 AND SER-648, 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Prostate cancer; RX PubMed=17487921; DOI=10.1002/elps.200600782; RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; RT "Toward a global characterization of the phosphoproteome in prostate cancer RT cells: identification of phosphoproteins in the LNCaP cell line."; RL Electrophoresis 28:2027-2034(2007). RN [10] RP 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 [11] RP FUNCTION, AND IDENTIFICATION IN THE SNARP COMPLEX. RX PubMed=18794151; DOI=10.1158/0008-5472.can-08-1217; RA Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M., Perkins N.D.; RT "Regulation of cyclin D1 RNA stability by SNIP1."; RL Cancer Res. 68:7621-7628(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-222; SER-264; RP SER-268; TYR-284; SER-290; THR-341; SER-385; SER-389; SER-397; THR-402; RP SER-512; SER-531; SER-578 AND SER-658, 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-397, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-222; SER-290; RP SER-385; SER-397; THR-402 AND SER-512, AND IDENTIFICATION BY MASS RP 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 [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152 AND LYS-437, AND RP IDENTIFICATION BY MASS 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-104; SER-177; RP SER-196; SER-198; SER-222; SER-268; SER-290; SER-297; SER-385; SER-397; RP THR-402; SER-472; SER-496; SER-502; SER-512; SER-531; THR-566; SER-578; RP SER-658 AND SER-690, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [19] 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-196; SER-198; RP SER-222; SER-268; SER-285; SER-290; SER-385; SER-397; THR-494; SER-496; RP SER-512; SER-531; SER-658; SER-660 AND SER-760, AND IDENTIFICATION BY MASS RP 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 [21] RP IDENTIFICATION IN A MACOM-LIKE COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=24100041; DOI=10.1074/jbc.m113.500397; RA Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T., RA Hamakubo T.; RT "Identification of Wilms' tumor 1-associating protein complex and its role RT in alternative splicing and the cell cycle."; RL J. Biol. Chem. 288:33292-33302(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-196; SER-198; RP SER-222; SER-259; SER-262; SER-264; SER-268; SER-285; SER-290; SER-300; RP SER-315; THR-341; THR-355; TYR-383; SER-385; SER-397; THR-402; SER-422; RP SER-427; THR-431; SER-450; SER-472; SER-496; SER-512; SER-525; SER-531; RP SER-559; SER-564; SER-578; SER-658; SER-660; THR-661 AND SER-690, 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; TYR-219; SER-222; RP SER-259; SER-264; SER-285; SER-290; SER-385; SER-389; SER-397; SER-648 AND RP SER-658, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339 (ISOFORM 4), 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 [24] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-809, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-332; LYS-413; LYS-437; LYS-462; RP LYS-491; LYS-501; LYS-548; LYS-550; LYS-580; LYS-676; LYS-778 AND LYS-831, RP AND 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-580 AND LYS-831, 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 [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-491; LYS-580; LYS-676 AND RP LYS-831, AND 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-421; LYS-437; LYS-457; LYS-501; RP LYS-536; LYS-548; LYS-550; LYS-580 AND LYS-676, AND IDENTIFICATION BY MASS RP 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-188; LYS-332; LYS-413; LYS-421; RP LYS-437; LYS-457; LYS-462; LYS-491; LYS-492; LYS-501; LYS-536; LYS-548; RP LYS-550; LYS-567; LYS-580; LYS-593; LYS-599; LYS-622; LYS-676; LYS-778; RP LYS-784; LYS-831 AND LYS-911, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 -!- FUNCTION: Death-promoting transcriptional repressor. May be involved in CC cyclin-D1/CCND1 mRNA stability through the SNARP complex which CC associates with both the 3'end of the CCND1 gene and its mRNA. CC {ECO:0000269|PubMed:18794151}. CC -!- SUBUNIT: Interacts with Bcl-2 related proteins, EMD, with the CC adenovirus E1B 19 kDa protein and with DNA. Component of the SNARP CC complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN. CC Component of a MACOM-like complex, named WTAP complex, composed of CC WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3. CC {ECO:0000269|PubMed:15009215, ECO:0000269|PubMed:18794151, CC ECO:0000269|PubMed:24100041}. CC -!- INTERACTION: CC Q9NYF8; P10415: BCL2; NbExp=2; IntAct=EBI-437804, EBI-77694; CC Q9NYF8; P50402: EMD; NbExp=3; IntAct=EBI-437804, EBI-489887; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus speckle CC {ECO:0000269|PubMed:24100041}. Nucleus, nucleoplasm CC {ECO:0000269|PubMed:24100041}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9NYF8-1; Sequence=Displayed; CC Name=2; Synonyms=Btf-l; CC IsoId=Q9NYF8-2; Sequence=VSP_010369; CC Name=3; Synonyms=Btf-s, BP-1; CC IsoId=Q9NYF8-3; Sequence=VSP_010369, VSP_010370; CC Name=4; CC IsoId=Q9NYF8-4; Sequence=VSP_010371; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- PTM: Citrullinated by PADI4. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the BCLAF1/THRAP3 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH47687.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH47887.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH56894.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH63846.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA11481.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/43164/BCLAF1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF249273; AAF64304.1; -; mRNA. DR EMBL; D79986; BAA11481.2; ALT_INIT; mRNA. DR EMBL; AL121713; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47950.1; -; Genomic_DNA. DR EMBL; CH471051; EAW47951.1; -; Genomic_DNA. DR EMBL; BC047687; AAH47687.1; ALT_SEQ; mRNA. DR EMBL; BC047887; AAH47887.1; ALT_SEQ; mRNA. DR EMBL; BC056894; AAH56894.1; ALT_SEQ; mRNA. DR EMBL; BC063846; AAH63846.1; ALT_SEQ; mRNA. DR EMBL; BC132780; AAI32781.1; -; mRNA. DR EMBL; BC144281; AAI44282.1; -; mRNA. DR CCDS; CCDS47485.1; -. [Q9NYF8-4] DR CCDS; CCDS47486.1; -. [Q9NYF8-3] DR CCDS; CCDS5177.1; -. [Q9NYF8-1] DR CCDS; CCDS75525.1; -. [Q9NYF8-2] DR RefSeq; NP_001070908.1; NM_001077440.1. [Q9NYF8-3] DR RefSeq; NP_001070909.1; NM_001077441.1. [Q9NYF8-4] DR RefSeq; NP_001287967.1; NM_001301038.1. [Q9NYF8-2] DR RefSeq; NP_055554.1; NM_014739.2. [Q9NYF8-1] DR PDB; 7RJN; X-ray; 1.95 A; C/D=330-339. DR PDB; 7RJR; X-ray; 1.45 A; B=330-339. DR PDBsum; 7RJN; -. DR PDBsum; 7RJR; -. DR AlphaFoldDB; Q9NYF8; -. DR SMR; Q9NYF8; -. DR BioGRID; 115118; 305. DR ComplexPortal; CPX-2653; SNIP1/SkIP associated RNA-processing complex. DR IntAct; Q9NYF8; 132. DR MINT; Q9NYF8; -. DR STRING; 9606.ENSP00000435210; -. DR GlyGen; Q9NYF8; 10 sites, 1 O-linked glycan (10 sites). DR iPTMnet; Q9NYF8; -. DR MetOSite; Q9NYF8; -. DR PhosphoSitePlus; Q9NYF8; -. DR SwissPalm; Q9NYF8; -. DR BioMuta; BCLAF1; -. DR DMDM; 47605556; -. DR EPD; Q9NYF8; -. DR jPOST; Q9NYF8; -. DR MassIVE; Q9NYF8; -. DR MaxQB; Q9NYF8; -. DR PaxDb; 9606-ENSP00000435210; -. DR PeptideAtlas; Q9NYF8; -. DR ProteomicsDB; 83221; -. [Q9NYF8-1] DR ProteomicsDB; 83222; -. [Q9NYF8-2] DR ProteomicsDB; 83223; -. [Q9NYF8-3] DR ProteomicsDB; 83224; -. [Q9NYF8-4] DR Pumba; Q9NYF8; -. DR Antibodypedia; 1744; 365 antibodies from 32 providers. DR DNASU; 9774; -. DR Ensembl; ENST00000353331.8; ENSP00000229446.5; ENSG00000029363.17. [Q9NYF8-3] DR Ensembl; ENST00000392348.6; ENSP00000376159.2; ENSG00000029363.17. [Q9NYF8-3] DR Ensembl; ENST00000527759.5; ENSP00000434826.1; ENSG00000029363.17. [Q9NYF8-2] DR Ensembl; ENST00000530767.5; ENSP00000436501.1; ENSG00000029363.17. [Q9NYF8-4] DR Ensembl; ENST00000531224.6; ENSP00000435210.1; ENSG00000029363.17. [Q9NYF8-1] DR GeneID; 9774; -. DR KEGG; hsa:9774; -. DR MANE-Select; ENST00000531224.6; ENSP00000435210.1; NM_014739.3; NP_055554.1. DR UCSC; uc003qgw.2; human. [Q9NYF8-1] DR AGR; HGNC:16863; -. DR CTD; 9774; -. DR DisGeNET; 9774; -. DR GeneCards; BCLAF1; -. DR HGNC; HGNC:16863; BCLAF1. DR HPA; ENSG00000029363; Tissue enhanced (bone). DR MIM; 612588; gene. DR neXtProt; NX_Q9NYF8; -. DR OpenTargets; ENSG00000029363; -. DR PharmGKB; PA134868035; -. DR VEuPathDB; HostDB:ENSG00000029363; -. DR eggNOG; ENOG502QZG7; Eukaryota. DR GeneTree; ENSGT00950000183163; -. DR HOGENOM; CLU_014485_0_0_1; -. DR InParanoid; Q9NYF8; -. DR OMA; KEENQKX; -. DR OrthoDB; 5323286at2759; -. DR PhylomeDB; Q9NYF8; -. DR TreeFam; TF335939; -. DR PathwayCommons; Q9NYF8; -. DR SignaLink; Q9NYF8; -. DR SIGNOR; Q9NYF8; -. DR BioGRID-ORCS; 9774; 635 hits in 1125 CRISPR screens. DR ChiTaRS; BCLAF1; human. DR GeneWiki; BCLAF1; -. DR GenomeRNAi; 9774; -. DR Pharos; Q9NYF8; Tbio. DR PRO; PR:Q9NYF8; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9NYF8; Protein. DR Bgee; ENSG00000029363; Expressed in calcaneal tendon and 211 other cell types or tissues. DR ExpressionAtlas; Q9NYF8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016592; C:mediator complex; IBA:GO_Central. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl. DR GO; GO:0006974; P:DNA damage response; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI. DR GO; GO:2000144; P:positive regulation of DNA-templated transcription initiation; IMP:UniProtKB. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR InterPro; IPR029199; THRAP3_BCLAF1. DR PANTHER; PTHR15268:SF4; BCL-2-ASSOCIATED TRANSCRIPTION FACTOR 1; 1. DR PANTHER; PTHR15268; THRAP3/BCLAF1; 1. DR Pfam; PF15440; THRAP3_BCLAF1; 1. DR Genevisible; Q9NYF8; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Citrullination; Cytoplasm; KW Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation; KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..920 FT /note="Bcl-2-associated transcription factor 1" FT /id="PRO_0000064888" FT REGION 1..437 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 464..502 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 637..796 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 810..840 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 862..920 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..18 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 19..42 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 43..67 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 93..135 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 136..156 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 157..200 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 234..295 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 331..398 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 637..750 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 763..787 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 104 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 152 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 177 FT /note="Phosphoserine" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 181 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 198 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 219 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 222 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 ECO:0007744|PubMed:24275569" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 262 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 264 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 284 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 285 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 290 FT /note="Phosphoserine" FT /evidence="ECO:0000269|Ref.6, 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 297 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 300 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 315 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 332 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K019" FT MOD_RES 341 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 355 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 383 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 385 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 ECO:0007744|PubMed:24275569" FT MOD_RES 389 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569" FT MOD_RES 397 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720, 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 402 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 421 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K019" FT MOD_RES 422 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 431 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 437 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 450 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 472 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 475 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K019" FT MOD_RES 494 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 496 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 502 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 512 FT /note="Phosphoserine" FT /evidence="ECO:0000269|Ref.6, 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 525 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 531 FT /note="Phosphoserine" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 559 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 564 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 566 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 578 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 648 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:24275569" FT MOD_RES 658 FT /note="Phosphoserine" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 660 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 661 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 690 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 760 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 803 FT /note="Citrulline" FT /evidence="ECO:0000250" FT MOD_RES 809 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT CROSSLNK 188 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 332 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 CROSSLNK 413 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 421 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 437 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 457 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 462 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 491 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 492 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 501 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 536 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 548 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 550 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 567 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 580 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 580 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 593 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 599 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 622 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 676 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 778 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 784 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 831 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 831 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 911 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 35..36 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10330179, FT ECO:0000303|PubMed:15489334" FT /id="VSP_010369" FT VAR_SEQ 339..511 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010371" FT VAR_SEQ 800..848 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10330179" FT /id="VSP_010370" FT VARIANT 66 FT /note="G -> A (in dbSNP:rs9942517)" FT /id="VAR_059591" FT VARIANT 209 FT /note="S -> C (in dbSNP:rs6940018)" FT /id="VAR_050692" FT VARIANT 459 FT /note="Y -> D (in dbSNP:rs1967446)" FT /id="VAR_050693" FT VARIANT 461 FT /note="L -> H (in dbSNP:rs1967445)" FT /id="VAR_050694" FT VARIANT 629 FT /note="N -> S (in dbSNP:rs7381749)" FT /id="VAR_050695" FT VARIANT 875 FT /note="R -> C (in dbSNP:rs34541670)" FT /id="VAR_050696" FT CONFLICT 4 FT /note="S -> A (in Ref. 1; AAF64304)" FT /evidence="ECO:0000305" FT MOD_RES Q9NYF8-4:339 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" SQ SEQUENCE 920 AA; 106122 MW; 8892B98E54F52C20 CRC64; MGRSNSRSHS SRSKSRSQSS SRSRSRSHSR KKRYSSRSRS RTYSRSRSRD RMYSRDYRRD YRNNRGMRRP YGYRGRGRGY YQGGGGRYHR GGYRPVWNRR HSRSPRRGRS RSRSPKRRSV SSQRSRSRSR RSYRSSRSPR SSSSRSSSPY SKSPVSKRRG SQEKQTKKAE GEPQEESPLK SKSQEEPKDT FEHDPSESID EFNKSSATSG DIWPGLSAYD NSPRSPHSPS PIATPPSQSS SCSDAPMLST VHSAKNTPSQ HSHSIQHSPE RSGSGSVGNG SSRYSPSQNS PIHHIPSRRS PAKTIAPQNA PRDESRGRSS FYPDGGDQET AKTGKFLKRF TDEESRVFLL DRGNTRDKEA SKEKGSEKGR AEGEWEDQEA LDYFSDKESG KQKFNDSEGD DTEETEDYRQ FRKSVLADQG KSFATASHRN TEEEGLKYKS KVSLKGNRES DGFREEKNYK LKETGYVVER PSTTKDKHKE EDKNSERITV KKETQSPEQV KSEKLKDLFD YSPPLHKNLD AREKSTFREE SPLRIKMIAS DSHRPEVKLK MAPVPLDDSN RPASLTKDRL LASTLVHSVK KEQEFRSIFD HIKLPQASKS TSESFIQHIV SLVHHVKEQY FKSAAMTLNE RFTSYQKATE EHSTRQKSPE IHRRIDISPS TLRKHTRLAG EERVFKEENQ KGDKKLRCDS ADLRHDIDRR RKERSKERGD SKGSRESSGS RKQEKTPKDY KEYKSYKDDS KHKREQDHSR SSSSSASPSS PSSREEKESK KEREEEFKTH HEMKEYSGFA GVSRPRGTFF RIRGRGRARG VFAGTNTGPN NSNTTFQKRP KEEEWDPEYT PKSKKYFLHD DRDDGVDYWA KRGRGRGTFQ RGRGRFNFKK SGSSPKWTHD KYQGDGIVED EEETMENNEE KKDRRKEEKE //