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Database: UniProt
Entry: G3UYK2_MOUSE
LinkDB: G3UYK2_MOUSE
Original site: G3UYK2_MOUSE 
ID   G3UYK2_MOUSE            Unreviewed;       949 AA.
AC   G3UYK2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=MDS1 and EVI1 complex locus {ECO:0000313|Ensembl:ENSMUSP00000134117.2};
DE   Flags: Fragment;
GN   Name=Mecom {ECO:0000313|Ensembl:ENSMUSP00000134117.2,
GN   ECO:0000313|MGI:MGI:95457};
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 {ECO:0000313|Ensembl:ENSMUSP00000134117.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000134117.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000134117.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [3] {ECO:0000313|Ensembl:ENSMUSP00000134117.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000134117.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G3UYK2; -.
DR   SMR; G3UYK2; -.
DR   MaxQB; G3UYK2; -.
DR   ProteomicsDB; 328255; -.
DR   Antibodypedia; 18615; 459 antibodies from 35 providers.
DR   Ensembl; ENSMUST00000172697.8; ENSMUSP00000134117.2; ENSMUSG00000027684.17.
DR   AGR; MGI:95457; -.
DR   MGI; MGI:95457; Mecom.
DR   VEuPathDB; HostDB:ENSMUSG00000027684; -.
DR   GeneTree; ENSGT00940000157208; -.
DR   ChiTaRS; Mecom; mouse.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000027684; Expressed in urinary bladder urothelium and 236 other cell types or tissues.
DR   ExpressionAtlas; G3UYK2; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24393:SF15; IP01201P-RELATED; 1.
DR   PANTHER; PTHR24393; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF21549; PRDM2_PR; 1.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   Pfam; PF13912; zf-C2H2_6; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   1: Evidence at protein level;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Proteomics identification {ECO:0007829|ProteomicsDB:G3UYK2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          80..192
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          211..239
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          265..292
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          293..320
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          321..349
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          350..377
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          378..405
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          407..434
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          923..949
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          22..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..777
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..808
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         949
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000134117.2"
SQ   SEQUENCE   949 AA;  106107 MW;  AF8A506C0F926189 CRC64;
     MRSKGRARKL ATSNECAYGN YPEIPLEEMP DADADGITSV PSLHIQEPCS PATSSESFTP
     KEGSPYKAPI YIPDDIPIPD EFELRESTMP GAGLGIWTKR KIEIGEKFGP YMGEQRSDLK
     DSSYGWEILD EFCNVKFCID ASQPDVGSWL KYIRFAGCYD QHNLVACQIN DQIFYRVVAD
     IAPGEELLLF MKSEEDPHEP MAPDIHEERQ HRCEDCDQLF ESKAELADHQ KFPCSTPHSA
     FSMVEEDLQQ NLESESDLRE IHGNQDCKEC DRVFPDLQSL EKHMLSHTEE REYKCDQCPK
     AFNWKSNLIR HQMSHDSGKH YECENCAKVF TDPSNLQRHI RSQHVGARAH ACPECGKTFA
     TSSGLKQHKH IHSSVKPFIC EVCHKSYTQF SNLCRHKRMH ADCRTQIKCK DCGQMFSTTS
     SLNKHRRFCE GKNHFAAGGF FGQGISLPGT PAMDKTSMVN MSHANPGLAD YFGTNRHPAG
     LTFPTAPGFS FSFPGLFPSG LYHRPPLIPA SPPVKGLSST EQSNKCQSPL LTHPQILPAT
     QDILKALSKH PPVGDNKPVE LLPERSSEER PLEKISDQSE SSDLDDVSTP SGSDLETTSG
     SDLESDLESD KEKCKENGKM FKDKVSPLQN LASITNKKEH NNHSVFSASV EEQSAVSGAV
     NDSIKAIASI AEKYFGSTGL VGLQDKKVGA LPYPSMFPLP FFPAFSQSMY PFPDRDLRSL
     PLKMEPQSPS EVKKLQKGSS ESPFDLTTKR KDEKPLTSGP SKPSGTPATS QDQPLDLSMG
     SRGRASGTKL TEPRKNHVFG EKKGSNMDTR PSSDGSLQHA RPTPFFMDPI YRVEKRKLTD
     PLEALKEKYL RPSPGFLFHP QFPLPDQRTW MSAIENMAEK LESFSALKPE ASELLQSVPS
     MFSFRAPPNT LPENLLRKGK ERYTCRYCGK IFPRSANLTR HLRTHTGEQ
//
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