MYEF2_HUMAN
ID MYEF2_HUMAN Reviewed; 600 AA.
AC Q9P2K5; A7MCZ9; C9J921; C9K0J4; Q6NUM5; Q7L388; Q7Z4B7; Q9H922; Q9NUQ1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Myelin expression factor 2;
DE Short=MEF-2;
DE Short=MyEF-2;
DE AltName: Full=MST156;
GN Name=MYEF2; Synonyms=KIAA1341;
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 MRNA] (ISOFORM 1), AND VARIANTS THR-91 AND
RP ARG-426.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP THR-91; ARG-426 AND GLY-465.
RC TISSUE=Placenta, and Teratocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 364-600 (ISOFORM 2), AND VARIANTS THR-91 AND
RP ARG-426.
RC TISSUE=Bone marrow, and 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-582 (ISOFORM 2), AND VARIANTS THR-91;
RP ARG-426 AND GLY-465.
RC TISSUE=Aorta;
RA Hui R.T., Sheng H., Qin B.M., Liu B., Zhao B., Liu Y.Q., Zhang Q., Song L.,
RA Liu B.H., Lu H., Wang X.Y.;
RT "Homo sapiens normal aorta mRNA MST156, complete cds.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-431, AND
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13 AND SER-17, 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY MASS
RP 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: Transcriptional repressor of the myelin basic protein gene
CC (MBP). Binds to the proximal MB1 element 5'-TTGTCC-3' of the MBP
CC promoter. Its binding to MB1 and function are inhibited by PURA (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9P2K5-2; Q96MW5: COG8; NbExp=3; IntAct=EBI-10318831, EBI-720875;
CC Q9P2K5-2; Q08379: GOLGA2; NbExp=6; IntAct=EBI-10318831, EBI-618309;
CC Q9P2K5-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10318831, EBI-739832;
CC Q9P2K5-2; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-10318831, EBI-10271199;
CC Q9P2K5-2; O43482: OIP5; NbExp=5; IntAct=EBI-10318831, EBI-536879;
CC Q9P2K5-2; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-10318831, EBI-949255;
CC Q9P2K5-2; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-10318831, EBI-742397;
CC Q9P2K5-2; Q13077: TRAF1; NbExp=3; IntAct=EBI-10318831, EBI-359224;
CC Q9P2K5-2; P36406: TRIM23; NbExp=3; IntAct=EBI-10318831, EBI-740098;
CC Q9P2K5-2; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-10318831, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9P2K5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2K5-2; Sequence=VSP_013454;
CC Name=3;
CC IsoId=Q9P2K5-3; Sequence=VSP_013451, VSP_013454;
CC Name=4;
CC IsoId=Q9P2K5-4; Sequence=VSP_013452, VSP_013453;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14533.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ13703.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA92579.1; 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; AB037762; BAA92579.1; ALT_INIT; mRNA.
DR EMBL; AK002075; BAA92070.1; -; mRNA.
DR EMBL; AK023133; BAB14421.1; -; mRNA.
DR EMBL; AC066612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014533; AAH14533.3; ALT_INIT; mRNA.
DR EMBL; BC068523; AAH68523.1; -; mRNA.
DR EMBL; BC152420; AAI52421.1; -; mRNA.
DR EMBL; BC152451; AAI52452.1; -; mRNA.
DR EMBL; AF190159; AAQ13703.1; ALT_FRAME; mRNA.
DR CCDS; CCDS32230.1; -. [Q9P2K5-1]
DR CCDS; CCDS73722.1; -. [Q9P2K5-2]
DR RefSeq; NP_001288139.1; NM_001301210.1.
DR RefSeq; NP_057216.2; NM_016132.4.
DR AlphaFoldDB; Q9P2K5; -.
DR SMR; Q9P2K5; -.
DR BioGRID; 119124; 117.
DR IntAct; Q9P2K5; 40.
DR MINT; Q9P2K5; -.
DR STRING; 9606.ENSP00000316950; -.
DR iPTMnet; Q9P2K5; -.
DR MetOSite; Q9P2K5; -.
DR PhosphoSitePlus; Q9P2K5; -.
DR BioMuta; MYEF2; -.
DR DMDM; 296439294; -.
DR EPD; Q9P2K5; -.
DR jPOST; Q9P2K5; -.
DR MassIVE; Q9P2K5; -.
DR MaxQB; Q9P2K5; -.
DR PaxDb; Q9P2K5; -.
DR PeptideAtlas; Q9P2K5; -.
DR PRIDE; Q9P2K5; -.
DR ProteomicsDB; 83833; -. [Q9P2K5-1]
DR ProteomicsDB; 83834; -. [Q9P2K5-2]
DR ProteomicsDB; 83835; -. [Q9P2K5-3]
DR ProteomicsDB; 83836; -. [Q9P2K5-4]
DR DNASU; 50804; -.
DR Ensembl; ENST00000561151.1; ENSP00000452913.1; ENSG00000104177.19. [Q9P2K5-4]
DR Ensembl; ENST00000561351.5; ENSP00000453125.1; ENSG00000104177.19. [Q9P2K5-4]
DR GeneID; 50804; -.
DR KEGG; hsa:50804; -.
DR UCSC; uc059iwz.1; human. [Q9P2K5-1]
DR CTD; 50804; -.
DR DisGeNET; 50804; -.
DR GeneCards; MYEF2; -.
DR HGNC; HGNC:17940; MYEF2.
DR MalaCards; MYEF2; -.
DR MIM; 619395; gene.
DR neXtProt; NX_Q9P2K5; -.
DR OpenTargets; ENSG00000104177; -.
DR PharmGKB; PA134877084; -.
DR VEuPathDB; HostDB:ENSG00000104177; -.
DR eggNOG; ENOG502QV3I; Eukaryota.
DR GeneTree; ENSGT00940000157397; -.
DR HOGENOM; CLU_1980808_0_0_1; -.
DR InParanoid; Q9P2K5; -.
DR OrthoDB; 1174365at2759; -.
DR PhylomeDB; Q9P2K5; -.
DR TreeFam; TF313406; -.
DR PathwayCommons; Q9P2K5; -.
DR SignaLink; Q9P2K5; -.
DR BioGRID-ORCS; 50804; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; MYEF2; human.
DR GenomeRNAi; 50804; -.
DR Pharos; Q9P2K5; Tdark.
DR PRO; PR:Q9P2K5; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9P2K5; protein.
DR Bgee; ENSG00000104177; Expressed in ventricular zone and 166 other tissues.
DR ExpressionAtlas; Q9P2K5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0014902; P:myotube differentiation; IEP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEP:UniProtKB.
DR GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd12658; RRM1_MYEF2; 1.
DR CDD; cd12662; RRM3_MYEF2; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034632; MYEF2.
DR InterPro; IPR034630; MYEF2_RRM1.
DR InterPro; IPR034631; MYEF2_RRM3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23003:SF15; PTHR23003:SF15; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Transcription; Ubl conjugation.
FT CHAIN 1..600
FT /note="Myelin expression factor 2"
FT /id="PRO_0000081655"
FT DOMAIN 100..178
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 233..310
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 523..599
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 406
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8C854"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 53
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..388
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013451"
FT VAR_SEQ 124..128
FT /note="VGEVT -> GLWCG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013452"
FT VAR_SEQ 129..600
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013453"
FT VAR_SEQ 437..460
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_013454"
FT VARIANT 91
FT /note="A -> T (in dbSNP:rs8023906)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.5"
FT /id="VAR_052209"
FT VARIANT 426
FT /note="Q -> R (in dbSNP:rs2470103)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.5"
FT /id="VAR_061829"
FT VARIANT 465
FT /note="S -> G (in dbSNP:rs36075490)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_052210"
FT CONFLICT 186
FT /note="L -> S (in Ref. 2; BAB14421)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="M -> G (in Ref. 4; AAH14533)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="A -> T (in Ref. 5; AAQ13703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 64122 MW; C965138A61B62DC3 CRC64;
MADANKAEVP GATGGDSPHL QPAEPPGEPR REPHPAEAEK QQPQHSSSSN GVKMENDESA
KEEKSDLKEK STGSKKANRF HPYSKDKNSG AGEKKGPNRN RVFISNIPYD MKWQAIKDLM
REKVGEVTYV ELFKDAEGKS RGCGVVEFKD EEFVKKALET MNKYDLSGRP LNIKEDPDGE
NARRALQRTG GSFPGGHVPD MGSGLMNLPP SILNNPNIPP EVISNLQAGR LGSTIFVANL
DFKVGWKKLK EVFSIAGTVK RADIKEDKDG KSRGMGTVTF EQAIEAVQAI SMFNGQFLFD
RPMHVKMDDK SVPHEEYRSH DGKTPQLPRG LGGIGMGLGP GGQPISASQL NIGGVMGNLG
PGGMGMDGPG FGGMNRIGGG IGFGGLEAMN SMGGFGGVGR MGELYRGAMT SSMERDFGRG
DIGINQGFGD SFGRLGSAMI GGFAGRIGSS NMGPVGSGIS GGMGSMNSVT GGMGMGLDRM
SSSFDRMGPG IGAILERSID MDRGFLSGPM GSGMRERIGS KGNQIFVRNL PFDLTWQKLK
EKFSQCGHVM FAEIKMENGK SKGCGTVRFD SPESAEKACR IMNGIKISGR EIDVRLDRNA
