ID TADA3_HUMAN Reviewed; 432 AA. AC O75528; Q6FI83; Q9UFS2; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 189. DE RecName: Full=Transcriptional adapter 3; DE AltName: Full=ADA3 homolog; DE Short=hADA3; DE AltName: Full=STAF54; DE AltName: Full=Transcriptional adapter 3-like; DE Short=ADA3-like protein; GN Name=TADA3; Synonyms=ADA3, TADA3L; 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 1), SUBCELLULAR LOCATION, AND RP INTERACTION WITH PCAF; TAF5L; TAF6L; TAF9; TAF10 AND TAF12. RX PubMed=9674425; DOI=10.1016/s0092-8674(00)81219-2; RA Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T., Yang X.-J., RA Howard B.H., Qin J., Nakatani Y.; RT "Histone-like TAFs within the PCAF histone acetylase complex."; RL Cell 94:35-44(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon mucosa; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Muscle, and Pancreas; 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 IDENTIFICATION IN THE STAGA COMPLEX, SUBCELLULAR LOCATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=11564863; DOI=10.1128/mcb.21.20.6782-6795.2001; RA Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., RA Kundu T.K., Chait B.T., Roeder R.G.; RT "Human STAGA complex is a chromatin-acetylating transcription coactivator RT that interacts with pre-mRNA splicing and DNA damage-binding factors in RT vivo."; RL Mol. Cell. Biol. 21:6782-6795(2001). RN [8] RP INTERACTION WITH TP53 AND THE HIGH-RISK HPV ONCOPROTEIN E6. RX PubMed=12138191; DOI=10.1128/mcb.22.16.5801-5812.2002; RA Kumar A., Zhao Y., Meng G., Zeng M., Srinivasan S., Delmolino L.M., Gao Q., RA Dimri G., Weber G.F., Wazer D.E., Band H., Band V.; RT "Human papillomavirus oncoprotein E6 inactivates the transcriptional RT coactivator human ADA3."; RL Mol. Cell. Biol. 22:5801-5812(2002). RN [9] RP FUNCTION, AND INTERACTION WITH TP53. RX PubMed=11707411; DOI=10.1093/emboj/20.22.6404; RA Wang T., Kobayashi T., Takimoto R., Denes A.E., Snyder E.L., el-Deiry W.S., RA Brachmann R.K.; RT "hADA3 is required for p53 activity."; RL EMBO J. 20:6404-6413(2001). RN [10] RP REVIEW, AND PCAF COMPLEX COMPOSITION. RX PubMed=9674419; DOI=10.1016/s0092-8674(00)81213-1; RA Struhl K., Moqtaderi Z.; RT "The TAFs in the HAT."; RL Cell 94:1-4(1998). RN [11] RP IDENTIFICATION IN THE TFTC-HAT COMPLEX. RX PubMed=12601814; DOI=10.1002/pmic.200390030; RA Cavusoglu N., Brand M., Tora L., van Dorsselaer A.; RT "Novel subunits of the TATA binding protein free TAFII-containing RT transcription complex identified by matrix-assisted laser RT desorption/ionization-time of flight mass spectrometry following one- RT dimensional gel electrophoresis."; RL Proteomics 3:217-223(2003). RN [12] RP FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX. RX PubMed=19103755; DOI=10.1128/mcb.01599-08; RA Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., RA Lill J.R., Zha J.; RT "The double-histone-acetyltransferase complex ATAC is essential for RT mammalian development."; RL Mol. Cell. Biol. 29:1176-1188(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-298, 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 [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-129, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- FUNCTION: Functions as a component of the PCAF complex. The PCAF CC complex is capable of efficiently acetylating histones in a nucleosomal CC context. The PCAF complex could be considered as the human version of CC the yeast SAGA complex. Also known as a coactivator for p53/TP53- CC dependent transcriptional activation. Component of the ATAC complex, a CC complex with histone acetyltransferase activity on histones H3 and H4. CC {ECO:0000269|PubMed:11707411, ECO:0000269|PubMed:19103755}. CC -!- SUBUNIT: The PCAF complex is composed of a number of TBP-associated CC factors (TAFS), such as TAF5, TAF5L, TAF6, TAF6L, TAF9, TAF10 and CC TAF12, PCAF, and also PCAF-associated factors (PAFs), such as CC TADA2L/ADA2, TADA3L/ADA3 and SPT3. Interacts directly with TADA2L and CC PCAF and also with the high-risk HPV oncoprotein E6. Component of the CC STAGA transcription coactivator-HAT complex, at least composed of CC SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, CC TRRAP and TAF9. Component of the TFTC-HAT complex. Component of the CC ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, CC TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. CC {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:11707411, CC ECO:0000269|PubMed:12138191, ECO:0000269|PubMed:12601814, CC ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:9674425}. CC -!- INTERACTION: CC O75528; Q9NY61: AATF; NbExp=2; IntAct=EBI-473249, EBI-372428; CC O75528; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-473249, EBI-12170453; CC O75528; P24863: CCNC; NbExp=3; IntAct=EBI-473249, EBI-395261; CC O75528; P28329-3: CHAT; NbExp=3; IntAct=EBI-473249, EBI-25837549; CC O75528; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-473249, EBI-5460660; CC O75528; P01112: HRAS; NbExp=3; IntAct=EBI-473249, EBI-350145; CC O75528; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-473249, EBI-6398041; CC O75528; O14901: KLF11; NbExp=3; IntAct=EBI-473249, EBI-948266; CC O75528; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-473249, EBI-2811583; CC O75528; Q8N2W9: PIAS4; NbExp=2; IntAct=EBI-473249, EBI-473160; CC O75528; P28702-3: RXRB; NbExp=3; IntAct=EBI-473249, EBI-16429492; CC O75528; Q96ES7: SGF29; NbExp=12; IntAct=EBI-473249, EBI-743117; CC O75528; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-473249, EBI-5235340; CC O75528; O75558: STX11; NbExp=3; IntAct=EBI-473249, EBI-714135; CC O75528; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-473249, EBI-6116822; CC O75528; P45974: USP5; NbExp=2; IntAct=EBI-473249, EBI-741277; CC O75528; Q8BWQ5: Dclk3; Xeno; NbExp=2; IntAct=EBI-473249, EBI-16518538; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, CC ECO:0000269|PubMed:9674425}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75528-1; Sequence=Displayed; CC Name=2; CC IsoId=O75528-2; Sequence=VSP_009739; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC -!- SIMILARITY: Belongs to the NGG1 family. {ECO:0000305}. 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; AF069733; AAC39903.1; -; mRNA. DR EMBL; AL117487; CAB55957.1; -; mRNA. DR EMBL; AK000228; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CR533543; CAG38574.1; -; mRNA. DR EMBL; CH471055; EAW63994.1; -; Genomic_DNA. DR EMBL; BC009240; AAH09240.1; -; mRNA. DR EMBL; BC013433; AAH13433.1; -; mRNA. DR CCDS; CCDS2583.1; -. [O75528-1] DR CCDS; CCDS2584.1; -. [O75528-2] DR PIR; T17267; T17267. DR RefSeq; NP_001265199.1; NM_001278270.1. [O75528-1] DR RefSeq; NP_006345.1; NM_006354.3. [O75528-1] DR RefSeq; NP_597814.1; NM_133480.2. [O75528-2] DR AlphaFoldDB; O75528; -. DR SMR; O75528; -. DR BioGRID; 115737; 138. DR ComplexPortal; CPX-1004; PCAF-containing ATAC complex. DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant. DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant. DR ComplexPortal; CPX-903; TFTC histone acetylation complex. DR ComplexPortal; CPX-989; PCAF histone acetylase complex. DR ComplexPortal; CPX-997; GCN5-containing ATAC complex. DR CORUM; O75528; -. DR IntAct; O75528; 91. DR MINT; O75528; -. DR STRING; 9606.ENSP00000307684; -. DR iPTMnet; O75528; -. DR PhosphoSitePlus; O75528; -. DR BioMuta; TADA3; -. DR EPD; O75528; -. DR jPOST; O75528; -. DR MassIVE; O75528; -. DR MaxQB; O75528; -. DR PaxDb; 9606-ENSP00000307684; -. DR PeptideAtlas; O75528; -. DR ProteomicsDB; 50064; -. [O75528-1] DR ProteomicsDB; 50065; -. [O75528-2] DR Pumba; O75528; -. DR Antibodypedia; 10290; 282 antibodies from 28 providers. DR DNASU; 10474; -. DR Ensembl; ENST00000301964.7; ENSP00000307684.2; ENSG00000171148.14. [O75528-1] DR Ensembl; ENST00000343450.2; ENSP00000343649.2; ENSG00000171148.14. [O75528-2] DR Ensembl; ENST00000440161.5; ENSP00000393471.1; ENSG00000171148.14. [O75528-1] DR GeneID; 10474; -. DR KEGG; hsa:10474; -. DR MANE-Select; ENST00000301964.7; ENSP00000307684.2; NM_006354.5; NP_006345.1. DR UCSC; uc003bsx.3; human. [O75528-1] DR AGR; HGNC:19422; -. DR CTD; 10474; -. DR DisGeNET; 10474; -. DR GeneCards; TADA3; -. DR HGNC; HGNC:19422; TADA3. DR HPA; ENSG00000171148; Low tissue specificity. DR MIM; 602945; gene. DR neXtProt; NX_O75528; -. DR OpenTargets; ENSG00000171148; -. DR PharmGKB; PA165698494; -. DR VEuPathDB; HostDB:ENSG00000171148; -. DR eggNOG; KOG4191; Eukaryota. DR GeneTree; ENSGT00390000008947; -. DR HOGENOM; CLU_038515_0_0_1; -. DR InParanoid; O75528; -. DR OMA; TPNKFWA; -. DR OrthoDB; 12488at2759; -. DR PhylomeDB; O75528; -. DR TreeFam; TF323397; -. DR PathwayCommons; O75528; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-9772755; Formation of WDR5-containing histone-modifying complexes. DR SignaLink; O75528; -. DR SIGNOR; O75528; -. DR BioGRID-ORCS; 10474; 351 hits in 1183 CRISPR screens. DR ChiTaRS; TADA3; human. DR GeneWiki; TADA3L; -. DR GenomeRNAi; 10474; -. DR Pharos; O75528; Tbio. DR PRO; PR:O75528; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; O75528; Protein. DR Bgee; ENSG00000171148; Expressed in right adrenal gland and 202 other cell types or tissues. DR ExpressionAtlas; O75528; baseline and differential. DR GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL. DR GO; GO:0072686; C:mitotic spindle; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB. DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB. DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB. DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0006325; P:chromatin organization; IEA:Ensembl. DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; TAS:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal. DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal. DR GO; GO:0006282; P:regulation of DNA repair; NAS:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:ComplexPortal. DR GO; GO:0045995; P:regulation of embryonic development; ISO:ComplexPortal. DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl. DR GO; GO:0043484; P:regulation of RNA splicing; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal. DR InterPro; IPR019340; Histone_AcTrfase_su3. DR PANTHER; PTHR13556:SF2; TRANSCRIPTIONAL ADAPTER 3; 1. DR PANTHER; PTHR13556; TRANSCRIPTIONAL ADAPTER 3-RELATED; 1. DR Pfam; PF10198; Ada3; 1. DR Genevisible; O75528; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..432 FT /note="Transcriptional adapter 3" FT /id="PRO_0000072416" FT REGION 87..126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 272..319 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 40..69 FT /evidence="ECO:0000255" FT COILED 367..407 FT /evidence="ECO:0000255" FT COMPBIAS 87..109 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 MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 298 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 418 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 21 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 129 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 370..432 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11230166, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4" FT /id="VSP_009739" FT CONFLICT 168 FT /note="E -> G (in Ref. 3; AK000228)" FT /evidence="ECO:0000305" SQ SEQUENCE 432 AA; 48902 MW; C86153CFA83F9226 CRC64; MSELKDCPLQ FHDFKSVDHL KVCPRYTAVL ARSEDDGIGI EELDTLQLEL ETLLSSASRR LRVLEAETQI LTDWQDKKGD RRFLKLGRDH ELGAPPKHGK PKKQKLEGKA GHGPGPGPGR PKSKNLQPKI QEYEFTDDPI DVPRIPKNDA PNRFWASVEP YCADITSEEV RTLEELLKPP EDEAEHYKIP PLGKHYSQRW AQEDLLEEQK DGARAAAVAD KKKGLMGPLT ELDTKDVDAL LKKSEAQHEQ PEDGCPFGAL TQRLLQALVE ENIISPMEDS PIPDMSGKES GADGASTSPR NQNKPFSVPH TKSLESRIKE ELIAQGLLES EDRPAEDSED EVLAELRKRQ AELKALSAHN RTKKHDLLRL AKEEVSRQEL RQRVRMADNE VMDAFRKIMA ARQKKRTPTK KEKDQAWKTL KERESILKLL DG //