MDEAS_HUMAN
ID MDEAS_HUMAN Reviewed; 1045 AA.
AC Q6PJG2; Q6PK13; Q6PK59; Q6ZS23;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Mitotic deacetylase-associated SANT domain protein {ECO:0000312|HGNC:HGNC:19853};
DE AltName: Full=ELM2 and SANT domain-containing protein 1;
GN Name=MIDEAS {ECO:0000303|PubMed:25653165, ECO:0000312|HGNC:HGNC:19853};
GN Synonyms=C14orf117 {ECO:0000312|HGNC:HGNC:19853},
GN C14orf43 {ECO:0000312|HGNC:HGNC:19853},
GN ELMSAN1 {ECO:0000312|HGNC:HGNC:19853};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1024, AND VARIANT LEU-554.
RC TISSUE=Muscle, Skin, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1019.
RC TISSUE=Brain;
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 IDENTIFICATION BY MASS 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; THR-704 AND THR-715, AND
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; THR-655; SER-661;
RP THR-704; SER-709 AND THR-715, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, 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 [9]
RP INTERACTION WITH DNTTIP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21573134; DOI=10.1371/journal.pgen.1002065;
RA Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L.,
RA Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.;
RT "Nuclear cGMP-dependent kinase regulates gene expression via activity-
RT dependent recruitment of a conserved histone deacetylase complex.";
RL PLoS Genet. 7:E1002065-E1002065(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND IDENTIFICATION BY
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-923, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-704 AND THR-715, 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 [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-193 AND ARG-447, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-590, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [16]
RP INTERACTION WITH DNTTIP1, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25653165; DOI=10.1093/nar/gkv068;
RA Itoh T., Fairall L., Muskett F.W., Milano C.P., Watson P.J., Arnaudo N.,
RA Saleh A., Millard C.J., El-Mezgueldi M., Martino F., Schwabe J.W.;
RT "Structural and functional characterization of a cell cycle associated
RT HDAC1/2 complex reveals the structural basis for complex assembly and
RT nucleosome targeting.";
RL Nucleic Acids Res. 43:2033-2044(2015).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-166 AND LYS-590, 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 -!- SUBUNIT: Interacts with DNTTIP1 (PubMed:21573134, PubMed:25653165).
CC Identified in a histone deacetylase complex that contains DNTTIP1,
CC HDAC1 and MIDEAS; this complex assembles into a tetramer that contains
CC four copies of each protein chain (PubMed:25653165).
CC {ECO:0000269|PubMed:21573134, ECO:0000269|PubMed:25653165}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06511.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AC006146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006511; AAH06511.1; ALT_INIT; mRNA.
DR EMBL; BC009202; AAH09202.1; -; mRNA.
DR EMBL; BC015668; AAH15668.1; -; mRNA.
DR EMBL; AK127785; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS9819.1; -.
DR RefSeq; NP_001036783.1; NM_001043318.2.
DR RefSeq; NP_919254.2; NM_194278.3.
DR PDB; 6Z2J; EM; 4.00 A; D/F=717-887.
DR PDB; 6Z2K; EM; 4.50 A; D/F/J/L=717-887.
DR PDBsum; 6Z2J; -.
DR PDBsum; 6Z2K; -.
DR AlphaFoldDB; Q6PJG2; -.
DR SMR; Q6PJG2; -.
DR BioGRID; 124872; 82.
DR CORUM; Q6PJG2; -.
DR IntAct; Q6PJG2; 71.
DR MINT; Q6PJG2; -.
DR STRING; 9606.ENSP00000286523; -.
DR GlyGen; Q6PJG2; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; Q6PJG2; -.
DR MetOSite; Q6PJG2; -.
DR PhosphoSitePlus; Q6PJG2; -.
DR BioMuta; ELMSAN1; -.
DR DMDM; 118572229; -.
DR EPD; Q6PJG2; -.
DR jPOST; Q6PJG2; -.
DR MassIVE; Q6PJG2; -.
DR MaxQB; Q6PJG2; -.
DR PaxDb; Q6PJG2; -.
DR PeptideAtlas; Q6PJG2; -.
DR PRIDE; Q6PJG2; -.
DR ProteomicsDB; 67201; -.
DR Antibodypedia; 167; 26 antibodies from 13 providers.
DR DNASU; 91748; -.
DR Ensembl; ENST00000286523.9; ENSP00000286523.5; ENSG00000156030.14.
DR Ensembl; ENST00000394071.6; ENSP00000377634.2; ENSG00000156030.14.
DR GeneID; 91748; -.
DR KEGG; hsa:91748; -.
DR UCSC; uc001xot.4; human.
DR CTD; 91748; -.
DR DisGeNET; 91748; -.
DR GeneCards; MIDEAS; -.
DR HGNC; HGNC:19853; MIDEAS.
DR HPA; ENSG00000156030; Low tissue specificity.
DR neXtProt; NX_Q6PJG2; -.
DR OpenTargets; ENSG00000156030; -.
DR VEuPathDB; HostDB:ENSG00000156030; -.
DR eggNOG; KOG4167; Eukaryota.
DR GeneTree; ENSGT00940000157459; -.
DR HOGENOM; CLU_011395_0_0_1; -.
DR InParanoid; Q6PJG2; -.
DR OMA; NHSMVFG; -.
DR PhylomeDB; Q6PJG2; -.
DR TreeFam; TF106431; -.
DR PathwayCommons; Q6PJG2; -.
DR SignaLink; Q6PJG2; -.
DR BioGRID-ORCS; 91748; 38 hits in 1095 CRISPR screens.
DR ChiTaRS; ELMSAN1; human.
DR GenomeRNAi; 91748; -.
DR Pharos; Q6PJG2; Tdark.
DR PRO; PR:Q6PJG2; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q6PJG2; protein.
DR Bgee; ENSG00000156030; Expressed in sural nerve and 179 other tissues.
DR ExpressionAtlas; Q6PJG2; baseline and differential.
DR Genevisible; Q6PJG2; HS.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF01448; ELM2; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA-binding; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1045
FT /note="Mitotic deacetylase-associated SANT domain protein"
FT /id="PRO_0000259764"
FT DOMAIN 721..813
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 828..879
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 193
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 447
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 655
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 704
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 715
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 86
FT /note="A -> V (in dbSNP:rs35302179)"
FT /id="VAR_050182"
FT VARIANT 554
FT /note="P -> L (in dbSNP:rs17782124)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_050183"
FT VARIANT 895
FT /note="D -> N (in dbSNP:rs35905570)"
FT /id="VAR_061361"
FT CONFLICT 626
FT /note="N -> D (in Ref. 2; AAH09202)"
FT /evidence="ECO:0000305"
FT CONFLICT 1020
FT /note="E -> K (in Ref. 2; AAH09202/AAH15668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1045 AA; 114989 MW; 1FFD4CE7557D026F CRC64;
MNLQAQPKAQ NKRKRCLFGG QEPAPKEQPP PLQPPQQSIR VKEEQYLGHE GPGGAVSTSQ
PVELPPPSSL ALLNSVVYGP ERTSAAMLSQ QVASVKWPNS VMAPGRGPER GGGGGVSDSS
WQQQPGQPPP HSTWNCHSLS LYSATKGSPH PGVGVPTYYN HPEALKREKA GGPQLDRYVR
PMMPQKVQLE VGRPQAPLNS FHAAKKPPNQ SLPLQPFQLA FGHQVNRQVF RQGPPPPNPV
AAFPPQKQQQ QQQPQQQQQQ QQAALPQMPL FENFYSMPQQ PSQQPQDFGL QPAGPLGQSH
LAHHSMAPYP FPPNPDMNPE LRKALLQDSA PQPALPQVQI PFPRRSRRLS KEGILPPSAL
DGAGTQPGQE ATGNLFLHHW PLQQPPPGSL GQPHPEALGF PLELRESQLL PDGERLAPNG
REREAPAMGS EEGMRAVSTG DCGQVLRGGV IQSTRRRRRA SQEANLLTLA QKAVELASLQ
NAKDGSGSEE KRKSVLASTT KCGVEFSEPS LATKRAREDS GMVPLIIPVS VPVRTVDPTE
AAQAGGLDED GKGPEQNPAE HKPSVIVTRR RSTRIPGTDA QAQAEDMNVK LEGEPSVRKP
KQRPRPEPLI IPTKAGTFIA PPVYSNITPY QSHLRSPVRL ADHPSERSFE LPPYTPPPIL
SPVREGSGLY FNAIISTSTI PAPPPITPKS AHRTLLRTNS AEVTPPVLSV MGEATPVSIE
PRINVGSRFQ AEIPLMRDRA LAAADPHKAD LVWQPWEDLE SSREKQRQVE DLLTAACSSI
FPGAGTNQEL ALHCLHESRG DILETLNKLL LKKPLRPHNH PLATYHYTGS DQWKMAERKL
FNKGIAIYKK DFFLVQKLIQ TKTVAQCVEF YYTYKKQVKI GRNGTLTFGD VDTSDEKSAQ
EEVEVDIKTS QKFPRVPLPR RESPSEERLE PKREVKEPRK EGEEEVPEIQ EKEEQEEGRE
RSRRAAAVKA TQTLQANESA SDILILRSHE SNAPGSAGGQ ASEKPREGTG KSRRALPFSE
KKKKTETFSK TQNQENTFPC KKCGR
