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Protein SET (Phosphatase 2A inhibitor I2PP2A) (I-2PP2A) (Template-activating factor I) (TAF-I)

 SET_MOUSE               Reviewed;         289 AA.
Q9EQU5; A2BE95; Q9CY82; Q9D0A9; Q9Z181;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 136.
RecName: Full=Protein SET;
AltName: Full=Phosphatase 2A inhibitor I2PP2A;
Short=I-2PP2A;
AltName: Full=Template-activating factor I;
Short=TAF-I;
Name=Set;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6 X DBA/2; TISSUE=Blastocyst;
PubMed=11078917; DOI=10.1016/S0304-3835(00)00598-X;
Fukukawa C., Shima H., Tamura N., Ogawa K., Kikuchi K.;
"Up-regulation of I-2PP2A/SET gene expression in rat primary hepatomas
and regenerating livers.";
Cancer Lett. 161:89-95(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-222 (ISOFORM 2).
TISSUE=Embryo;
PubMed=11231286; DOI=10.1046/j.1432-1327.2001.02000.x;
Minakuchi M., Kakazu N., Gorrin-Rivas M.J., Abe T., Copeland T.D.,
Ueda K., Adachi Y.;
"Identification and characterization of SEB, a novel protein that
binds to the acute undifferentiated leukemia-associated protein SET.";
Eur. J. Biochem. 268:1340-1351(2001).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[7]
GLYCYLATION.
PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
Janke C.;
"Evolutionary divergence of enzymatic mechanisms for posttranslational
polyglycylation.";
Cell 137:1076-1087(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT ALA-2, AND
MUTAGENESIS OF LYS-4.
PubMed=20668449; DOI=10.1038/nature09343;
Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
"NRMT is an alpha-N-methyltransferase that methylates RCC1 and
retinoblastoma protein.";
Nature 466:1125-1128(2010).
[10]
INTERACTION WITH CHTOP.
PubMed=22872859; DOI=10.1074/mcp.M112.017194;
Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S.,
van Dijk T.B.;
"Five friends of methylated chromatin target of protein-arginine-
methyltransferase[prmt]-1 (chtop), a complex linking arginine
methylation to desumoylation.";
Mol. Cell. Proteomics 11:1263-1273(2012).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23 AND LYS-67, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Multitasking protein, involved in apoptosis,
transcription, nucleosome assembly and histone chaperoning.
Isoform 2 anti-apoptotic activity is mediated by inhibition of the
GZMA-activated DNase, NME1. In the course of cytotoxic T-
lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting
its binding to NME1 and releasing NME1 inhibition. Isoform 1 and
isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform
1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation
of histones (HAT) and nucleosomes, most probably by masking the
accessibility of lysines of histones to the acetylases. The
predominant target for inhibition is histone H4. HAT inhibition
leads to silencing of HAT-dependent transcription and prevents
active demethylation of DNA. Both isoforms stimulate DNA
replication of the adenovirus genome complexed with viral core
proteins; however, isoform 2 specific activity is higher (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Headphone-shaped homodimer. Isoform 1 and isoform 2
interact directly with each other and with ANP32A within the
tripartite INHAT (inhibitor of acetyltransferases) complex.
Isoform 1 and isoform 2 interact also with histones. Isoform 2 is
a omponent of the SET complex, composed of at least ANP32A, APEX1,
HMGB2, NME1, SET and TREX1, but not NME2 or TREX2. Within this
complex, directly interacts with ANP32A, NME1, HMGB2 and TREX1;
the interaction with ANP32A is enhanced after cleavage. Interacts
with APBB1, CHTOP, SETBP1, SGO1. {ECO:0000269|PubMed:22872859}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
Endoplasmic reticulum {ECO:0000250}. Nucleus, nucleoplasm
{ECO:0000250}. Note=In the cytoplasm, found both in the cytosol
and associated with the endoplasmic reticulum. The SET complex is
associated with the endoplasmic reticulum. Following CTL attack
and cleavage by GZMA, moves rapidly to the nucleus, where it is
found in the nucleoplasm, avoiding the nucleolus. Similar
translocation to the nucleus is also observed for lymphocyte-
activated killer cells after the addition of calcium (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=TAF-I alpha;
IsoId=Q9EQU5-1; Sequence=Displayed;
Name=2; Synonyms=TAF-I beta;
IsoId=Q9EQU5-2; Sequence=VSP_009869;
Note=Contains a N6-acetyllysine at position 11. Contains a
phosphoserine at position 15. Contains a phosphothreonine at
position 23. {ECO:0000250};
Name=3;
IsoId=Q9EQU5-3; Sequence=VSP_009870, VSP_009871;
-!- DOMAIN: A long alpha helix in the N-terminus mediates
dimerization, while the earmuff domain is responsible for core
histone and dsDNA binding. The C-terminal acidic domain mediates
the inhibition of histone acetyltransferases and is required for
the DNA replication stimulatory activity (By similarity).
{ECO:0000250}.
-!- PTM: Some glutamate residues are glycylated by TTLL8. This
modification occurs exclusively on glutamate residues and results
in a glycine chain on the gamma-carboxyl group.
-!- PTM: N-terminus of isoform 1 is methylated by METTL11A/NTM1.
Mainly trimethylated. {ECO:0000269|PubMed:20668449}.
-!- PTM: Isoform 2 is cleaved after Lys-176 by GZMA. The cleavage
inhibits its nucelosome assembly activity and disrupts the
inhibition on NME1 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP)
family. {ECO:0000305}.
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EMBL; AB044937; BAB20793.1; -; mRNA.
EMBL; AK011630; BAB27745.1; -; mRNA.
EMBL; AK019960; BAB31936.1; -; mRNA.
EMBL; BX005298; CAM18951.1; -; Genomic_DNA.
EMBL; BC018255; AAH18255.1; -; mRNA.
EMBL; AB015613; BAA34736.1; -; mRNA.
CCDS; CCDS15866.1; -. [Q9EQU5-1]
CCDS; CCDS57162.1; -. [Q9EQU5-2]
RefSeq; NP_001191804.1; NM_001204875.1. [Q9EQU5-2]
RefSeq; NP_076360.1; NM_023871.4. [Q9EQU5-1]
UniGene; Mm.326055; -.
UniGene; Mm.335942; -.
ProteinModelPortal; Q9EQU5; -.
SMR; Q9EQU5; -.
BioGrid; 207808; 101.
IntAct; Q9EQU5; 69.
MINT; MINT-1854783; -.
STRING; 10090.ENSMUSP00000099930; -.
iPTMnet; Q9EQU5; -.
PhosphoSitePlus; Q9EQU5; -.
EPD; Q9EQU5; -.
PaxDb; Q9EQU5; -.
PeptideAtlas; Q9EQU5; -.
PRIDE; Q9EQU5; -.
Ensembl; ENSMUST00000067996; ENSMUSP00000070002; ENSMUSG00000054766. [Q9EQU5-2]
Ensembl; ENSMUST00000102866; ENSMUSP00000099930; ENSMUSG00000054766. [Q9EQU5-1]
GeneID; 56086; -.
KEGG; mmu:56086; -.
UCSC; uc008jaw.2; mouse. [Q9EQU5-1]
UCSC; uc008jax.2; mouse. [Q9EQU5-3]
UCSC; uc008jay.2; mouse. [Q9EQU5-2]
CTD; 6418; -.
MGI; MGI:1860267; Set.
eggNOG; KOG1508; Eukaryota.
eggNOG; ENOG410XQRX; LUCA.
GeneTree; ENSGT00530000062882; -.
HOGENOM; HOG000232096; -.
HOVERGEN; HBG014779; -.
InParanoid; Q9EQU5; -.
KO; K11290; -.
OMA; PVALMNH; -.
OrthoDB; EOG091G00YT; -.
PhylomeDB; Q9EQU5; -.
TreeFam; TF313386; -.
Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
Reactome; R-MMU-450520; HuR (ELAVL1) binds and stabilizes mRNA.
PRO; PR:Q9EQU5; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000054766; -.
CleanEx; MM_SET; -.
ExpressionAtlas; Q9EQU5; baseline and differential.
Genevisible; Q9EQU5; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005811; C:lipid droplet; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
InterPro; IPR037231; NAP-like_sf.
InterPro; IPR002164; NAP_family.
PANTHER; PTHR11875; PTHR11875; 1.
Pfam; PF00956; NAP; 1.
SUPFAM; SSF143113; SSF143113; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chaperone; Complete proteome;
Cytoplasm; DNA-binding; Endoplasmic reticulum; Isopeptide bond;
Methylation; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:20668449}.
CHAIN 2 289 Protein SET.
/FTId=PRO_0000185663.
REGION 31 77 Dimerization. {ECO:0000250}.
REGION 78 224 Earmuff domain. {ECO:0000250}.
COMPBIAS 226 277 Asp/Glu-rich (highly acidic).
MOD_RES 2 2 N,N,N-trimethylalanine; by NTM1.
{ECO:0000269|PubMed:20668449}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:Q01105}.
MOD_RES 23 23 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000250|UniProtKB:Q01105}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000250|UniProtKB:Q01105}.
MOD_RES 67 67 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 145 145 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 149 149 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01105}.
MOD_RES 171 171 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01105}.
CROSSLNK 153 153 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q01105}.
VAR_SEQ 1 36 MAPKRQSAILPQPKKPRPAAAPKLEDKSASPGLPKG -> M
SAPTAKASKKELNSNHDGADETS (in isoform 2).
{ECO:0000303|PubMed:11231286,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_009869.
VAR_SEQ 83 146 RSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVE
VTEFEDIKSGYRIDFYFDENPYF -> STTWFPTWMMKKER
QKMMMTTTKRRRGWKILMKKEMRMKVKKMTMRMKGRKERRT
KARMISTED (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009870.
VAR_SEQ 147 289 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009871.
MUTAGEN 4 4 K->Q: Almost abolishes N-terminal
methylation at A-2.
{ECO:0000269|PubMed:20668449}.
CONFLICT 91 91 P -> L (in Ref. 5; BAA34736).
{ECO:0000305}.
CONFLICT 184 184 Q -> L (in Ref. 5; BAA34736).
{ECO:0000305}.
CONFLICT 207 207 D -> A (in Ref. 5; BAA34736).
{ECO:0000305}.
SEQUENCE 289 AA; 33378 MW; B8FDD71A78107019 CRC64;
MAPKRQSAIL PQPKKPRPAA APKLEDKSAS PGLPKGEKEQ QEAIEHIDEV QNEIDRLNEQ
ASEEILKVEQ KYNKLRQPFF QKRSELIAKI PNFWVTTFVN HPQVSALLGE EDEEALHYLT
RVEVTEFEDI KSGYRIDFYF DENPYFENKV LSKEFHLNES GDPSSKSTEI KWKSGKDLTK
RSSQTQNKAS RKRQHEEPES FFTWFTDHSD AGADELGEVI KDDIWPNPLQ YYLVPDMDDE
EGEAEDDDDD DEEEEGLEDI DEEGDEDEGE EDDDEDEGEE GEEDEGEDD


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