TADA3_HUMAN
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 03-AUG-2022, entry version 180.
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}.
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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; 127.
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; O75528; -.
DR PeptideAtlas; O75528; -.
DR PRIDE; O75528; -.
DR ProteomicsDB; 50064; -. [O75528-1]
DR ProteomicsDB; 50065; -. [O75528-2]
DR Antibodypedia; 10290; 249 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 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 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 SignaLink; O75528; -.
DR BioGRID-ORCS; 10474; 341 hits in 1103 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 200 other tissues.
DR ExpressionAtlas; O75528; baseline and differential.
DR Genevisible; O75528; HS.
DR GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL.
DR GO; GO:0072686; C:mitotic spindle; IC: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:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:ComplexPortal.
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:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA: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; IC:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IC:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; IMP: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; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal.
DR InterPro; IPR019340; Histone_AcTrfase_su3.
DR PANTHER; PTHR13556; PTHR13556; 2.
DR Pfam; PF10198; Ada3; 1.
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
