SET_HUMAN
ID SET_HUMAN Reviewed; 290 AA.
AC Q01105; A5A5H4; A6NGV1; B4DUE2; Q15541; Q5VXV1; Q5VXV2; Q6FHZ5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Protein SET;
DE AltName: Full=HLA-DR-associated protein II;
DE AltName: Full=Inhibitor of granzyme A-activated DNase;
DE Short=IGAAD;
DE AltName: Full=PHAPII;
DE AltName: Full=Phosphatase 2A inhibitor I2PP2A;
DE Short=I-2PP2A;
DE AltName: Full=Template-activating factor I;
DE Short=TAF-I;
GN Name=SET;
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).
RX PubMed=1630450; DOI=10.1128/mcb.12.8.3346-3355.1992;
RA von Lindern M., van Baal S., Wiegant J., Raap A., Hagemeijer A.,
RA Grosveld G.;
RT "Can, a putative oncogene associated with myeloid leukemogenesis, may be
RT activated by fusion of its 3' half to different genes: characterization of
RT the set gene.";
RL Mol. Cell. Biol. 12:3346-3355(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8192856; DOI=10.1515/bchm3.1994.375.2.113;
RA Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T.,
RA Zimmermann B., Kratzin H.D., Hilschmann N.;
RT "Purification and characterization of two putative HLA class II associated
RT proteins: PHAPI and PHAPII.";
RL Biol. Chem. Hoppe-Seyler 375:113-126(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 14-35;
RP 40-60; 75-90 AND 155-167, AND ACTIVATION OF DNA REPLICATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=7753797; DOI=10.1073/pnas.92.10.4279;
RA Nagata K., Kawase H., Handa H., Yano K., Yamasaki M., Ishimi Y., Okuda A.,
RA Kikuchi A., Matsumoto K.;
RT "Replication factor encoded by a putative oncogene, set, associated with
RT myeloid leukemogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4279-4283(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=8626647; DOI=10.1074/jbc.271.19.11059;
RA Li M., Makkinje A., Damuni Z.;
RT "The myeloid leukemia-associated protein SET is a potent inhibitor of
RT protein phosphatase 2A.";
RL J. Biol. Chem. 271:11059-11062(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15642345; DOI=10.1016/j.febslet.2004.11.097;
RA Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K.;
RT "Inhibitors of protein phosphatase-2A from human brain structures,
RT immunocytological localization and activities towards dephosphorylation of
RT the Alzheimer type hyperphosphorylated tau.";
RL FEBS Lett. 579:363-372(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [11]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=8294483; DOI=10.1016/s0021-9258(17)42162-4;
RA Adachi Y., Pavlaki G.N., Copeland T.D.;
RT "Identification and characterization of SET, a nuclear phosphoprotein
RT encoded by the translocation break point in acute undifferentiated
RT leukemia.";
RL J. Biol. Chem. 269:2258-2262(1994).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-241 (ISOFORM 2).
RA Wang L.C., Chen Y.;
RT "A relative factor in human rectum carcinoma.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP EXPRESSION IN THE KIDNEY.
RX PubMed=9773788; DOI=10.1681/asn.v9101873;
RA Carlson S.G., Eng E., Kim E.-G., Perlman E.J., Copeland T.D.,
RA Ballermann B.J.;
RT "Expression of SET, an inhibitor of protein phosphatase 2A, in renal
RT development and Wilms' tumor.";
RL J. Am. Soc. Nephrol. 9:1873-1880(1998).
RN [14]
RP INHIBITION OF HISTONE ACETYLATION.
RX PubMed=11163245; DOI=10.1016/s0092-8674(01)00196-9;
RA Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D.;
RT "Regulation of histone acetylation and transcription by INHAT, a human
RT cellular complex containing the Set oncoprotein.";
RL Cell 104:119-130(2001).
RN [15]
RP INTERACTION WITH SETBP1.
RC TISSUE=Cervix carcinoma;
RX PubMed=11231286; DOI=10.1046/j.1432-1327.2001.02000.x;
RA Minakuchi M., Kakazu N., Gorrin-Rivas M.J., Abe T., Copeland T.D., Ueda K.,
RA Adachi Y.;
RT "Identification and characterization of SEB, a novel protein that binds to
RT the acute undifferentiated leukemia-associated protein SET.";
RL Eur. J. Biochem. 268:1340-1351(2001).
RN [16]
RP FUNCTION, INTERACTION WITH ANP32A, PROTEOLYTIC CLEAVAGE AT LYS-179 BY GZMA
RP (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=11555662; DOI=10.1074/jbc.m108137200;
RA Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M.,
RA Lieberman J.;
RT "Granzyme A activates an endoplasmic reticulum-associated caspase-
RT independent nuclease to induce single-stranded DNA nicks.";
RL J. Biol. Chem. 276:43285-43293(2001).
RN [17]
RP INTERACTION WITH HMGB2, AND IDENTIFICATION IN THE SET COMPLEX.
RX PubMed=11909973; DOI=10.1128/mcb.22.8.2810-2820.2002;
RA Fan Z., Beresford P.J., Zhang D., Lieberman J.;
RT "HMG2 interacts with the nucleosome assembly protein SET and is a target of
RT the cytotoxic T-lymphocyte protease granzyme A.";
RL Mol. Cell. Biol. 22:2810-2820(2002).
RN [18]
RP FUNCTION IN NME1 INHIBITION, INTERACTION WITH NME1, SUBCELLULAR LOCATION,
RP DESCRIPTION OF THE SET COMPLEX, AND PROTEOLYTIC CLEAVAGE BY GZMA.
RX PubMed=12628186; DOI=10.1016/s0092-8674(03)00150-8;
RA Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.;
RT "Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-
RT mediated apoptosis, and the nucleosome assembly protein SET is its
RT inhibitor.";
RL Cell 112:659-672(2003).
RN [19]
RP ERRATUM OF PUBMED:12628186.
RA Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.;
RL Cell 115:241-241(2003).
RN [20]
RP INTERACTION WITH HERPES SIMPLEX VIRUS 1 VP22 (MICROBIAL INFECTION).
RX PubMed=12917472; DOI=10.1099/vir.0.19326-0;
RA van Leeuwen H., Okuwaki M., Hong R., Chakravarti D., Nagata K., O'Hare P.;
RT "Herpes simplex virus type 1 tegument protein VP22 interacts with TAF-I
RT proteins and inhibits nucleosome assembly but not regulation of histone
RT acetylation by INHAT.";
RL J. Gen. Virol. 84:2501-2510(2003).
RN [21]
RP SUBCELLULAR LOCATION.
RX PubMed=12524539; DOI=10.1038/ni885;
RA Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A.,
RA Pommier Y., Lieberman J.;
RT "Cleaving the oxidative repair protein Ape1 enhances cell death mediated by
RT granzyme A.";
RL Nat. Immunol. 4:145-153(2003).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [23]
RP INTERACTION WITH TREX1, IDENTIFICATION IN THE SET COMPLEX, PROTEOLYTIC
RP CLEAVAGE BY GZMA, AND SUBCELLULAR LOCATION.
RX PubMed=16818237; DOI=10.1016/j.molcel.2006.06.005;
RA Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B.,
RA Perrino F.W., Lieberman J.;
RT "The exonuclease TREX1 is in the SET complex and acts in concert with NM23-
RT H1 to degrade DNA during granzyme A-mediated cell death.";
RL Mol. Cell 23:133-142(2006).
RN [24]
RP INTERACTION WITH SGO1.
RX PubMed=16541025; DOI=10.1038/nature04663;
RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
RA Kawashima S.A., Watanabe Y.;
RT "Shugoshin collaborates with protein phosphatase 2A to protect cohesin.";
RL Nature 441:46-52(2006).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP 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 [26]
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 [27]
RP INTERACTION WITH APBB1.
RX PubMed=19343227; DOI=10.1371/journal.pone.0005071;
RA Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
RA Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
RT "FE65 binds Teashirt, inhibiting expression of the primate-specific
RT caspase-4.";
RL PLoS ONE 4:E5071-E5071(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150 AND LYS-172, ACETYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-11 (ISOFORM 2), 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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-15 AND SER-24 (ISOFORM 2), AND IDENTIFICATION BY
RP 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 [30]
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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-24 (ISOFORM 2),
RP AND IDENTIFICATION BY MASS 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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-63, 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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP 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 [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [35]
RP INVOLVEMENT IN MRD58, AND VARIANT MRD58 233-TYR--ASP-290 DEL.
RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L.,
RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E.,
RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S.,
RA Rouleau G.A., Michaud J.L.;
RT "De novo mutations in moderate or severe intellectual disability.";
RL PLoS Genet. 10:E1004772-E1004772(2014).
RN [36]
RP INVOLVEMENT IN MRD58, AND VARIANTS MRD58 GLY-95 AND TYR-118.
RX PubMed=29688601; DOI=10.1002/humu.23541;
RG CAUSES Study;
RA Stevens S.J.C., van der Schoot V., Leduc M.S., Rinne T., Lalani S.R.,
RA Weiss M.M., van Hagen J.M., Lachmeijer A.M.A., Stockler-Ipsiroglu S.G.,
RA Lehman A., Brunner H.G.;
RT "De novo mutations in the SET nuclear proto-oncogene, encoding a component
RT of the inhibitor of histone acetyltransferases (INHAT) complex in patients
RT with nonsyndromic intellectual disability.";
RL Hum. Mutat. 39:1014-1023(2018).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-238, DNA-BINDING, DOMAINS, AND
RP SUBUNIT.
RX PubMed=17360516; DOI=10.1073/pnas.0603762104;
RA Muto S., Senda M., Akai Y., Sato L., Suzuki T., Nagai R., Senda T.,
RA Horikoshi M.;
RT "Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone
RT chaperone activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4285-4290(2007).
CC -!- FUNCTION: Multitasking protein, involved in apoptosis, transcription,
CC nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic
CC activity is mediated by inhibition of the GZMA-activated DNase, NME1.
CC In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA
CC cleaves SET, disrupting its binding to NME1 and releasing NME1
CC inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein
CC phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-
CC mediated acetylation of histones (HAT) and nucleosomes, most probably
CC by masking the accessibility of lysines of histones to the acetylases.
CC The predominant target for inhibition is histone H4. HAT inhibition
CC leads to silencing of HAT-dependent transcription and prevents active
CC demethylation of DNA. Both isoforms stimulate DNA replication of the
CC adenovirus genome complexed with viral core proteins; however, isoform
CC 2 specific activity is higher. {ECO:0000269|PubMed:11555662,
CC ECO:0000269|PubMed:12628186}.
CC -!- SUBUNIT: Headphone-shaped homodimer. Isoforms 1 and 2 interact directly
CC with each other and with ANP32A within the tripartite INHAT (inhibitor
CC of acetyltransferases) complex. Isoform 1 and isoform 2 interact also
CC with histones. Isoform 2 is a component of the SET complex, composed of
CC at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1, but not NME2 or
CC TREX2. Within this complex, directly interacts with ANP32A, NME1, HMGB2
CC and TREX1; the interaction with ANP32A is enhanced after cleavage.
CC Interacts with APBB1, CHTOP, SETBP1, SGO1.
CC {ECO:0000269|PubMed:11231286, ECO:0000269|PubMed:11555662,
CC ECO:0000269|PubMed:11909973, ECO:0000269|PubMed:12628186,
CC ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:16818237,
CC ECO:0000269|PubMed:17360516, ECO:0000269|PubMed:19343227}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 1
CC VP22. {ECO:0000269|PubMed:12917472}.
CC -!- INTERACTION:
CC Q01105; Q6SJ93: FAM111B; NbExp=3; IntAct=EBI-1053182, EBI-6309082;
CC Q01105; Q12778: FOXO1; NbExp=5; IntAct=EBI-1053182, EBI-1108782;
CC Q01105; Q00987: MDM2; NbExp=2; IntAct=EBI-1053182, EBI-389668;
CC Q01105; P50222: MEOX2; NbExp=3; IntAct=EBI-1053182, EBI-748397;
CC Q01105; P10644: PRKAR1A; NbExp=2; IntAct=EBI-1053182, EBI-476431;
CC Q01105; P63000: RAC1; NbExp=8; IntAct=EBI-1053182, EBI-413628;
CC Q01105; O00560: SDCBP; NbExp=3; IntAct=EBI-1053182, EBI-727004;
CC Q01105; Q15573: TAF1A; NbExp=2; IntAct=EBI-1053182, EBI-2510647;
CC Q01105; Q53T94: TAF1B; NbExp=3; IntAct=EBI-1053182, EBI-1560239;
CC Q01105; Q15572: TAF1C; NbExp=4; IntAct=EBI-1053182, EBI-2510659;
CC Q01105; P20226: TBP; NbExp=4; IntAct=EBI-1053182, EBI-355371;
CC Q01105; Q9BT49: THAP7; NbExp=7; IntAct=EBI-1053182, EBI-741350;
CC Q01105; P17480: UBTF; NbExp=4; IntAct=EBI-1053182, EBI-396235;
CC Q01105-2; Q53HL2: CDCA8; NbExp=3; IntAct=EBI-7481343, EBI-979174;
CC Q01105-2; Q6SJ93: FAM111B; NbExp=3; IntAct=EBI-7481343, EBI-6309082;
CC Q01105-2; Q92993: KAT5; NbExp=3; IntAct=EBI-7481343, EBI-399080;
CC Q01105-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-7481343, EBI-11742507;
CC Q01105-2; P26367: PAX6; NbExp=3; IntAct=EBI-7481343, EBI-747278;
CC Q01105-2; P17252: PRKCA; NbExp=3; IntAct=EBI-7481343, EBI-1383528;
CC Q01105-2; Q9BWE0-4: REPIN1; NbExp=3; IntAct=EBI-7481343, EBI-24236508;
CC Q01105-2; O00560: SDCBP; NbExp=3; IntAct=EBI-7481343, EBI-727004;
CC Q01105-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-7481343, EBI-9090795;
CC Q01105-2; Q562F6-3: SGO2; NbExp=3; IntAct=EBI-7481343, EBI-12111430;
CC Q01105-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-7481343, EBI-5235340;
CC Q01105-2; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-7481343, EBI-12833746;
CC Q01105-2; Q9BT49: THAP7; NbExp=5; IntAct=EBI-7481343, EBI-741350;
CC Q01105-2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-7481343, EBI-11741437;
CC Q01105-2; P61981: YWHAG; NbExp=3; IntAct=EBI-7481343, EBI-359832;
CC Q01105-2; P17021: ZNF17; NbExp=3; IntAct=EBI-7481343, EBI-1105334;
CC Q01105-2; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-7481343, EBI-11962468;
CC Q01105-2; Q49A12: ZNF85; NbExp=3; IntAct=EBI-7481343, EBI-18141506;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum.
CC Nucleus, nucleoplasm. Note=In the cytoplasm, found both in the cytosol
CC and associated with the endoplasmic reticulum. The SET complex is
CC associated with the endoplasmic reticulum. Following CTL attack and
CC cleavage by GZMA, moves rapidly to the nucleus, where it is found in
CC the nucleoplasm, avoiding the nucleolus. Similar translocation to the
CC nucleus is also observed for lymphocyte-activated killer cells after
CC the addition of calcium.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=TAF-I alpha;
CC IsoId=Q01105-1; Sequence=Displayed;
CC Name=2; Synonyms=TAF-I beta;
CC IsoId=Q01105-2; Sequence=VSP_009868;
CC Name=3;
CC IsoId=Q01105-3; Sequence=VSP_045175;
CC Name=4;
CC IsoId=Q01105-4; Sequence=VSP_046741;
CC -!- TISSUE SPECIFICITY: Widely expressed. Low levels in quiescent cells
CC during serum starvation, contact inhibition or differentiation. Highly
CC expressed in Wilms' tumor.
CC -!- DOMAIN: A long alpha helix in the N-terminus mediates dimerization,
CC while the earmuff domain is responsible for core histone and dsDNA
CC binding. The C-terminal acidic domain mediates the inhibition of
CC histone acetyltransferases and is required for the DNA replication
CC stimulatory activity. {ECO:0000269|PubMed:17360516}.
CC -!- PTM: Isoform 2 is phosphorylated on Ser-15 and Ser-24.
CC -!- PTM: Isoform 2 is acetylated on Lys-11.
CC -!- PTM: Some glutamate residues are glycylated by TTLL8. This modification
CC occurs exclusively on glutamate residues and results in a glycine chain
CC on the gamma-carboxyl group (By similarity). {ECO:0000250}.
CC -!- PTM: N-terminus of isoform 1 is methylated by METTL11A/NTM1. Mainly
CC trimethylated (By similarity). {ECO:0000250}.
CC -!- PTM: [Isoform 2]: Cleaved after Lys-176 by GZMA. The cleavage inhibits
CC its nucleosome assembly activity and disrupts the inhibition on NME1.
CC {ECO:0000269|PubMed:11555662, ECO:0000269|PubMed:12628186,
CC ECO:0000269|PubMed:16818237}.
CC -!- DISEASE: Note=A chromosomal aberration involving SET is found in some
CC cases of acute undifferentiated leukemia (AUL). Translocation
CC t(6;9)(q21;q34.1) with NUP214/CAN.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 58
CC (MRD58) [MIM:618106]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRD58
CC patients show delayed development, intellectual disability, language
CC delay and speech impairment. Some patients have motor delay or
CC incoordination, and minor dysmorphic features.
CC {ECO:0000269|PubMed:25356899, ECO:0000269|PubMed:29688601}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SETID42272ch9q34.html";
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DR EMBL; M93651; AAA60318.1; -; mRNA.
DR EMBL; X75091; CAA52982.1; -; mRNA.
DR EMBL; D45198; BAA08139.1; -; mRNA.
DR EMBL; U51924; AAC50460.1; -; mRNA.
DR EMBL; AY349172; AAQ79833.1; -; mRNA.
DR EMBL; CR536543; CAG38780.1; -; mRNA.
DR EMBL; CR542050; CAG46847.1; -; mRNA.
DR EMBL; AK223556; BAD97276.1; -; mRNA.
DR EMBL; AK300609; BAG62304.1; -; mRNA.
DR EMBL; AL356481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032749; AAH32749.1; -; mRNA.
DR EMBL; EF534308; ABP96841.1; -; mRNA.
DR CCDS; CCDS48037.1; -. [Q01105-1]
DR CCDS; CCDS59149.1; -. [Q01105-4]
DR CCDS; CCDS6907.1; -. [Q01105-2]
DR PIR; A57984; A45018.
DR PIR; I59377; I59377.
DR RefSeq; NP_001116293.1; NM_001122821.1. [Q01105-1]
DR RefSeq; NP_001234929.1; NM_001248000.1. [Q01105-4]
DR RefSeq; NP_001234930.1; NM_001248001.1.
DR RefSeq; NP_003002.2; NM_003011.3. [Q01105-2]
DR PDB; 2E50; X-ray; 2.30 A; A/B/P/Q=38-238.
DR PDB; 7MTO; X-ray; 1.79 A; A=37-238.
DR PDBsum; 2E50; -.
DR PDBsum; 7MTO; -.
DR AlphaFoldDB; Q01105; -.
DR SMR; Q01105; -.
DR BioGRID; 112316; 252.
DR CORUM; Q01105; -.
DR DIP; DIP-33561N; -.
DR IntAct; Q01105; 158.
DR MINT; Q01105; -.
DR STRING; 9606.ENSP00000361777; -.
DR ChEMBL; CHEMBL4295798; -.
DR GlyGen; Q01105; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q01105; -.
DR PhosphoSitePlus; Q01105; -.
DR SwissPalm; Q01105; -.
DR BioMuta; SET; -.
DR DMDM; 46397790; -.
DR EPD; Q01105; -.
DR jPOST; Q01105; -.
DR MassIVE; Q01105; -.
DR MaxQB; Q01105; -.
DR PaxDb; Q01105; -.
DR PeptideAtlas; Q01105; -.
DR PRIDE; Q01105; -.
DR ProteomicsDB; 1156; -.
DR ProteomicsDB; 57917; -. [Q01105-1]
DR ProteomicsDB; 57918; -. [Q01105-2]
DR ProteomicsDB; 65617; -.
DR TopDownProteomics; Q01105-1; -. [Q01105-1]
DR TopDownProteomics; Q01105-2; -. [Q01105-2]
DR Antibodypedia; 3931; 396 antibodies from 39 providers.
DR DNASU; 6418; -.
DR Ensembl; ENST00000322030.13; ENSP00000318012.9; ENSG00000119335.18. [Q01105-2]
DR Ensembl; ENST00000372692.8; ENSP00000361777.4; ENSG00000119335.18. [Q01105-1]
DR Ensembl; ENST00000409104.7; ENSP00000387321.3; ENSG00000119335.18. [Q01105-4]
DR Ensembl; ENST00000686840.1; ENSP00000509032.1; ENSG00000119335.18. [Q01105-1]
DR GeneID; 6418; -.
DR KEGG; hsa:6418; -.
DR MANE-Select; ENST00000322030.13; ENSP00000318012.9; NM_003011.4; NP_003002.2. [Q01105-2]
DR UCSC; uc004bvu.5; human. [Q01105-1]
DR CTD; 6418; -.
DR DisGeNET; 6418; -.
DR GeneCards; SET; -.
DR HGNC; HGNC:10760; SET.
DR HPA; ENSG00000119335; Low tissue specificity.
DR MalaCards; SET; -.
DR MIM; 600960; gene.
DR MIM; 618106; phenotype.
DR neXtProt; NX_Q01105; -.
DR OpenTargets; ENSG00000119335; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA35678; -.
DR VEuPathDB; HostDB:ENSG00000119335; -.
DR eggNOG; KOG1508; Eukaryota.
DR GeneTree; ENSGT00940000153877; -.
DR HOGENOM; CLU_051687_4_0_1; -.
DR InParanoid; Q01105; -.
DR OMA; WPVALMN; -.
DR OrthoDB; 1191764at2759; -.
DR PhylomeDB; Q01105; -.
DR TreeFam; TF313386; -.
DR PathwayCommons; Q01105; -.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR SignaLink; Q01105; -.
DR SIGNOR; Q01105; -.
DR BioGRID-ORCS; 6418; 162 hits in 1086 CRISPR screens.
DR ChiTaRS; SET; human.
DR EvolutionaryTrace; Q01105; -.
DR GeneWiki; Protein_SET; -.
DR GenomeRNAi; 6418; -.
DR Pharos; Q01105; Tbio.
DR PRO; PR:Q01105; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q01105; protein.
DR Bgee; ENSG00000119335; Expressed in ganglionic eminence and 217 other tissues.
DR ExpressionAtlas; Q01105; baseline and differential.
DR Genevisible; Q01105; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; TAS:ProtInc.
DR GO; GO:0019888; F:protein phosphatase regulator activity; TAS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0035067; P:negative regulation of histone acetylation; TAS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; TAS:ProtInc.
DR GO; GO:0006337; P:nucleosome disassembly; TAS:UniProtKB.
DR InterPro; IPR037231; NAP-like_sf.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
DR SUPFAM; SSF143113; SSF143113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone;
KW Chromosomal rearrangement; Cytoplasm; Direct protein sequencing;
KW Disease variant; DNA-binding; Endoplasmic reticulum;
KW Host-virus interaction; Intellectual disability; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9EQU5"
FT CHAIN 2..290
FT /note="Protein SET"
FT /id="PRO_0000185662"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..78
FT /note="Dimerization"
FT REGION 79..225
FT /note="Earmuff domain"
FT REGION 158..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..290
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 283..284
FT /note="Breakpoint for translocation to form SET-CAN
FT oncogene"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQU5"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQU5"
FT MOD_RES 146
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQU5"
FT MOD_RES 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT VAR_SEQ 1..37
FT /note="MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG -> MSAPAAKVSKK
FT ELNSNHDGADETS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15642345, ECO:0000303|PubMed:1630450,
FT ECO:0000303|PubMed:7753797, ECO:0000303|PubMed:8192856,
FT ECO:0000303|PubMed:8626647, ECO:0000303|Ref.12,
FT ECO:0000303|Ref.6, ECO:0000303|Ref.7"
FT /id="VSP_009868"
FT VAR_SEQ 1..37
FT /note="MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG -> MPRSHQPPPPP
FT H (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045175"
FT VAR_SEQ 1..37
FT /note="MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG -> MGCRDLLPSLK
FT PTLL (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_046741"
FT VARIANT 95
FT /note="W -> G (in MRD58; dbSNP:rs1554776500)"
FT /evidence="ECO:0000269|PubMed:29688601"
FT /id="VAR_081147"
FT VARIANT 118
FT /note="H -> Y (in MRD58; dbSNP:rs1564360978)"
FT /evidence="ECO:0000269|PubMed:29688601"
FT /id="VAR_081148"
FT VARIANT 233..290
FT /note="Missing (in MRD58)"
FT /evidence="ECO:0000269|PubMed:25356899"
FT /id="VAR_078653"
FT HELIX 38..88
FT /evidence="ECO:0007829|PDB:7MTO"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:7MTO"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:7MTO"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:7MTO"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:7MTO"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:7MTO"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:7MTO"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:7MTO"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:7MTO"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:7MTO"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:7MTO"
FT TURN 210..214
FT /evidence="ECO:0007829|PDB:7MTO"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:7MTO"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:7MTO"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:7MTO"
FT MOD_RES Q01105-2:11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES Q01105-2:15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q01105-2:24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VARIANT Q01105-2:4
FT /note="P -> Q (in dbSNP:rs1141138)"
FT /evidence="ECO:0000305"
FT /id="VAR_082865"
SQ SEQUENCE 290 AA; 33489 MW; F4664118171EF230 CRC64;
MAPKRQSPLP PQKKKPRPPP ALGPEETSAS AGLPKKGEKE QQEAIEHIDE VQNEIDRLNE
QASEEILKVE QKYNKLRQPF FQKRSELIAK IPNFWVTTFV NHPQVSALLG EEDEEALHYL
TRVEVTEFED IKSGYRIDFY FDENPYFENK VLSKEFHLNE SGDPSSKSTE IKWKSGKDLT
KRSSQTQNKA SRKRQHEEPE SFFTWFTDHS DAGADELGEV IKDDIWPNPL QYYLVPDMDD
EEGEGEEDDD DDEEEEGLED IDEEGDEDEG EEDEDDDEGE EGEEDEGEDD
