ANM1_MOUSE
ID ANM1_MOUSE Reviewed; 371 AA.
AC Q9JIF0; Q99LS4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Protein arginine N-methyltransferase 1;
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q99873};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT1;
GN Name=Prmt1; Synonyms=Hrmt1l2, Mrmt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=10848611; DOI=10.1128/mcb.20.13.4859-4869.2000;
RA Pawlak M.R., Scherer C.A., Chen J., Roshon M.J., Ruley H.E.;
RT "Arginine N-methyltransferase 1 is required for early postimplantation
RT mouse development, but cells deficient in the enzyme are viable.";
RL Mol. Cell. Biol. 20:4859-4869(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [3]
RP FUNCTION, AND INTERACTION WITH NFATC2IP.
RX PubMed=15327772; DOI=10.1016/j.molcel.2004.06.042;
RA Mowen K.A., Schurter B.T., Fathman J.W., David M., Glimcher L.H.;
RT "Arginine methylation of NIP45 modulates cytokine gene expression in
RT effector T lymphocytes.";
RL Mol. Cell 15:559-571(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CHTOP,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Erythroblast;
RX PubMed=19858291; DOI=10.1128/mcb.00645-09;
RA van Dijk T.B., Gillemans N., Stein C., Fanis P., Demmers J.,
RA van de Corput M., Essers J., Grosveld F., Bauer U.M., Philipsen S.;
RT "Friend of Prmt1, a novel chromatin target of protein arginine
RT methyltransferases.";
RL Mol. Cell. Biol. 30:260-272(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH CHTOP, AND SUBCELLULAR LOCATION.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-134, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP UBIQUITINATION AT LYS-145, ACETYLATION AT LYS-228 AND LYS-233, AND
RP MUTAGENESIS OF LYS-145; ILE-227; LYS-228; ILE-232 AND LYS-233.
RX PubMed=28883095; DOI=10.1242/jcs.206904;
RA Lai Y., Li J., Li X., Zou C.;
RT "Lipopolysaccharide modulates p300 and Sirt1 to promote PRMT1 stability via
RT an SCFFbxl17-recognized acetyldegron.";
RL J. Cell Sci. 130:3578-3587(2017).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30321814; DOI=10.1016/j.isci.2018.09.023;
RA Murata K., Lu W., Hashimoto M., Ono N., Muratani M., Nishikata K.,
RA Kim J.D., Ebihara S., Ishida J., Fukamizu A.;
RT "PRMT1 Deficiency in Mouse Juvenile Heart Induces Dilated Cardiomyopathy
RT and Reveals Cryptic Alternative Splicing Products.";
RL IScience 8:200-213(2018).
CC -!- FUNCTION: Arginine methyltransferase that methylates (mono and
CC asymmetric dimethylation) the guanidino nitrogens of arginyl residues
CC present in proteins such as ESR1, histone H2, H3 and H4, ILF3, HNRNPA1,
CC HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1,
CC CHTOP and MAP3K5/ASK1 (PubMed:15327772, PubMed:19858291). Constitutes
CC the main enzyme that mediates monomethylation and asymmetric
CC dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a,
CC respectively), a specific tag for epigenetic transcriptional activation
CC (By similarity). May be involved in the regulation of TAF15
CC transcriptional activity, act as an activator of estrogen receptor
CC (ER)-mediated transactivation, play a key role in neurite outgrowth and
CC act as a negative regulator of megakaryocytic differentiation, by
CC modulating p38 MAPK pathway (By similarity). Methylates RBM15,
CC promoting ubiquitination and degradation of RBM15 (By similarity).
CC Methylates FOXO1 and retains it in the nucleus increasing its
CC transcriptional activity. Methylates CHTOP and this methylation is
CC critical for its 5-hydroxymethylcytosine (5hmC)-binding activity
CC (PubMed:19858291). Methylates MAP3K5/ASK1 at 'Arg-85' and 'Arg-87'
CC which promotes association of MAP3K5 with thioredoxin and negatively
CC regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 stimulation
CC and MAP3K5-induced activation of JNK (By similarity). Methylates H4R3
CC in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-
CC dependent manner (By similarity). Plays a role in regulating
CC alternative splicing in the heart (PubMed:30321814).
CC {ECO:0000250|UniProtKB:Q99873, ECO:0000269|PubMed:15327772,
CC ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:30321814}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000250|UniProtKB:Q99873};
CC -!- SUBUNIT: Homodimer and heterodimer with PRMT8. Homooctamer; individual
CC homodimers associates to form a homooctamer. Individual homodimers can
CC associate to form a homohexamer. Interacts with BTG1, BTG2 and IFNAR1.
CC Interacts with ILF3 and SUPT5H. Interacts with and methylates FOXO1,
CC leading to the nuclear retention of FOXO1 and the stimulation of FOXO1
CC transcriptional activity. Methylation of FOXO1 is increased upon
CC oxidative stress (By similarity). Interacts with NFATC2IP. Interacts
CC with and methylates CHTOP, thereby enabling the interaction of CHTOP
CC with the 5FMC complex. Interacts with and probably methylates ATXN2L
CC (By similarity). Component of the methylosome, a 20S complex containing
CC at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH (By
CC similarity). Interacts with DHX9 (via RGG region) (By similarity).
CC Interacts (via N-terminus) with HABP4 (By similarity). Interacts with
CC MAP3K5/ASK1; the interaction results in MAP3K5 methylation by PRMT1
CC which inhibits MAP3K5 activation (By similarity). Interacts with
CC TRIM48; the interaction results in ubiquitination of PRMT1 by TRIM48,
CC leading to PRMT1 proteasomal degradation and activation of MAP3K5 (By
CC similarity). {ECO:0000250|UniProtKB:Q99873,
CC ECO:0000269|PubMed:15327772, ECO:0000269|PubMed:19858291,
CC ECO:0000269|PubMed:22872859}.
CC -!- INTERACTION:
CC Q9JIF0; Q14DJ8: Axin1; NbExp=3; IntAct=EBI-519055, EBI-4312125;
CC Q9JIF0; Q9CY57: Chtop; NbExp=8; IntAct=EBI-519055, EBI-6393116;
CC Q9JIF0; Q60749: Khdrbs1; NbExp=2; IntAct=EBI-519055, EBI-519077;
CC Q9JIF0; O35182: Smad6; NbExp=3; IntAct=EBI-519055, EBI-4321242;
CC Q9JIF0-1; Q14DJ8: Axin1; NbExp=2; IntAct=EBI-4312217, EBI-4312125;
CC Q9JIF0-3; Q14DJ8: Axin1; NbExp=2; IntAct=EBI-4422829, EBI-4312125;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19858291,
CC ECO:0000269|PubMed:30321814}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:22872859}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:19858291}. Cytoplasm {ECO:0000269|PubMed:19858291}.
CC Note=Mostly found in the cytoplasm (PubMed:19858291). Colocalizes with
CC CHTOP within the nucleus (PubMed:19858291). Low levels detected also in
CC the chromatin fraction (PubMed:22872859). {ECO:0000269|PubMed:19858291,
CC ECO:0000269|PubMed:22872859}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9JIF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JIF0-2; Sequence=VSP_005210;
CC Name=3;
CC IsoId=Q9JIF0-3; Sequence=VSP_005211;
CC -!- TISSUE SPECIFICITY: Expressed in the heart where it is detected in both
CC cardiomyocytes and non-myocytes (at protein level).
CC {ECO:0000269|PubMed:30321814}.
CC -!- PTM: Polyubiquitinated at Lys-145 by the SCF(FBXL17) complex, leading
CC to its subsequent degradation (PubMed:28883095). Ubiquitination is
CC regulated by acetylation at Lys-228 and Lys-233 (PubMed:28883095).
CC Polyubiquitinated by E3 ubiquitin-protein ligase TRIM48, leading to
CC suppression of MAP3K5/ASK1 methylation and subsequent MAP3K5 activation
CC (By similarity). {ECO:0000250|UniProtKB:Q99873,
CC ECO:0000269|PubMed:28883095}.
CC -!- PTM: Acetylation at Lys-228 and Lys-233 regulates ubiquitination by the
CC SCF(FBXL17) complex. Acetylated at Lys-233 by p300/EP300. Deacetylated
CC at Lys-228 and Lys-233 by SIRT1. {ECO:0000269|PubMed:28883095}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in cardiomyocytes results in
CC dilated cardiomyopathy in juveniles and death within 60 days of birth
CC with aberrant splicing occurring in a number of genes including Ktn1,
CC Lmo7, Mef2a, Tmed2, Snap23, Sorbs1 and Ttn.
CC {ECO:0000269|PubMed:30321814}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; AF232716; AAF37292.1; -; mRNA.
DR EMBL; AF232717; AAF37293.1; -; mRNA.
DR EMBL; BC002249; AAH02249.1; -; mRNA.
DR CCDS; CCDS21222.1; -. [Q9JIF0-1]
DR CCDS; CCDS57547.1; -. [Q9JIF0-2]
DR RefSeq; NP_001239405.1; NM_001252476.1. [Q9JIF0-2]
DR RefSeq; NP_062804.1; NM_019830.3. [Q9JIF0-1]
DR AlphaFoldDB; Q9JIF0; -.
DR SMR; Q9JIF0; -.
DR BioGRID; 200423; 47.
DR CORUM; Q9JIF0; -.
DR IntAct; Q9JIF0; 17.
DR MINT; Q9JIF0; -.
DR STRING; 10090.ENSMUSP00000103474; -.
DR iPTMnet; Q9JIF0; -.
DR PhosphoSitePlus; Q9JIF0; -.
DR SwissPalm; Q9JIF0; -.
DR EPD; Q9JIF0; -.
DR MaxQB; Q9JIF0; -.
DR PaxDb; Q9JIF0; -.
DR PRIDE; Q9JIF0; -.
DR ProteomicsDB; 281988; -. [Q9JIF0-1]
DR ProteomicsDB; 281989; -. [Q9JIF0-2]
DR ProteomicsDB; 281990; -. [Q9JIF0-3]
DR Antibodypedia; 18668; 552 antibodies from 40 providers.
DR DNASU; 15469; -.
DR Ensembl; ENSMUST00000107843; ENSMUSP00000103474; ENSMUSG00000109324. [Q9JIF0-1]
DR Ensembl; ENSMUST00000207370; ENSMUSP00000147252; ENSMUSG00000109324. [Q9JIF0-2]
DR GeneID; 15469; -.
DR KEGG; mmu:15469; -.
DR UCSC; uc009gsg.2; mouse. [Q9JIF0-1]
DR CTD; 3276; -.
DR MGI; MGI:107846; Prmt1.
DR VEuPathDB; HostDB:ENSMUSG00000109324; -.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000154700; -.
DR InParanoid; Q9JIF0; -.
DR OMA; TTDRMEV; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q9JIF0; -.
DR TreeFam; TF300608; -.
DR BRENDA; 2.1.1.319; 3474.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 15469; 31 hits in 78 CRISPR screens.
DR PRO; PR:Q9JIF0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JIF0; protein.
DR Bgee; ENSMUSG00000109324; Expressed in 1st arch mandibular component and 270 other tissues.
DR ExpressionAtlas; Q9JIF0; baseline and differential.
DR Genevisible; Q9JIF0; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016275; F:[cytochrome c]-arginine N-methyltransferase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042054; F:histone methyltransferase activity; IDA:MGI.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; ISO:MGI.
DR GO; GO:0008170; F:N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008276; F:protein methyltransferase activity; IMP:MGI.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:MGI.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISO:MGI.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; ISS:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0030519; F:snoRNP binding; ISO:MGI.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:UniProtKB.
DR GO; GO:0043985; P:histone H4-R3 methylation; ISS:UniProtKB.
DR GO; GO:0016571; P:histone methylation; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0018216; P:peptidyl-arginine methylation; ISO:MGI.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; ISO:MGI.
DR GO; GO:0035247; P:peptidyl-arginine omega-N-methylation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:MGI.
DR GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; ISO:MGI.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006479; P:protein methylation; ISO:MGI.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Ubl conjugation.
FT CHAIN 1..371
FT /note="Protein arginine N-methyltransferase 1"
FT /id="PRO_0000212322"
FT DOMAIN 50..371
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 162
FT /evidence="ECO:0000250"
FT ACT_SITE 171
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 134
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:28883095"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:28883095"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99873"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99873"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28883095"
FT VAR_SEQ 1..29
FT /note="MAAAEAANCIMENFVATLANGMSLQPPLE -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005211"
FT VAR_SEQ 13..30
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10848611"
FT /id="VSP_005210"
FT MUTAGEN 145
FT /note="K->R: Increased stability of the protein caused by
FT impaired ubiquitination by the SCF(FBXL17) complex."
FT /evidence="ECO:0000269|PubMed:28883095"
FT MUTAGEN 212
FT /note="K->R: Increased stability of the protein."
FT /evidence="ECO:0000269|PubMed:28883095"
FT MUTAGEN 227
FT /note="I->D: Slightly reduced degradation, probably caused
FT by reduced ubiquitination by the SCF(FBXL17) complex."
FT /evidence="ECO:0000269|PubMed:28883095"
FT MUTAGEN 228
FT /note="K->Q: Mimicks residue acetylation; impaired
FT interaction with FBXL17, leading to decreased
FT ubiquitination by the SCF(FBXL17) complex."
FT /evidence="ECO:0000269|PubMed:28883095"
FT MUTAGEN 228
FT /note="K->R: Increased interaction with FBXL17, leading to
FT increased ubiquitination by the SCF(FBXL17) complex."
FT /evidence="ECO:0000269|PubMed:28883095"
FT MUTAGEN 232
FT /note="I->D: Slightly reduced degradation, probably caused
FT by reduced ubiquitination by the SCF(FBXL17) complex."
FT /evidence="ECO:0000269|PubMed:28883095"
FT MUTAGEN 233
FT /note="K->Q: Mimicks residue acetylation; increased
FT interaction with FBXL17, leading to increased
FT ubiquitination by the SCF(FBXL17) complex."
FT /evidence="ECO:0000269|PubMed:28883095"
FT MUTAGEN 233
FT /note="K->R: Impaired interaction with FBXL17, leading to
FT decreased ubiquitination by the SCF(FBXL17) complex."
FT /evidence="ECO:0000269|PubMed:28883095"
FT MUTAGEN 356
FT /note="K->R: Increased stability of the protein."
FT /evidence="ECO:0000269|PubMed:28883095"
SQ SEQUENCE 371 AA; 42436 MW; AEFCF63001B1A38C CRC64;
MAAAEAANCI MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK DYYFDSYAHF
GIHEEMLKDE VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG ARKVIGIECS
SISDYAVKIV KANKLDHVVT IIKGKVEEVE LPVEKVDIII SEWMGYCLFY ESMLNTVLHA
RDKWLAPDGL IFPDRATLYV TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV
DPKQLVTNAC LIKEVDIYTV KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG
FSTSPESPYT HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT IDLDFKGQLC
ELSCSTDYRM R
