ZMYM3_MOUSE
ID ZMYM3_MOUSE Reviewed; 1370 AA.
AC Q9JLM4; Q80U17;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Zinc finger MYM-type protein 3;
DE AltName: Full=DXHXS6673E protein;
DE AltName: Full=Zinc finger protein 261;
GN Name=Zmym3; Synonyms=Kiaa0385, Zfp261, Znf261;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10662551; DOI=10.1006/geno.1999.6027;
RA Scheer M.P., van der Maarel S.M., Kuebart S., Schulz A., Wirth J.,
RA Schweiger S., Ropers H.-H., Nothwang H.G.;
RT "DXS6673E encodes a predominantly nuclear protein, and its mouse ortholog
RT DXHXS6673E is alternatively spliced in a developmental- and tissue-specific
RT manner.";
RL Genomics 63:123-132(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND SER-269, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. {ECO:0000250}.
CC -!- SUBUNIT: May be a component of a BHC histone deacetylase complex that
CC contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST,
CC PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9JLM4; Q9UHL9: GTF2IRD1; Xeno; NbExp=3; IntAct=EBI-12517169, EBI-372530;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10662551}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all embryonic stages and
CC adult tissues. {ECO:0000269|PubMed:10662551}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65550.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF156605; AAF37800.1; -; mRNA.
DR EMBL; AK122268; BAC65550.3; ALT_INIT; Transcribed_RNA.
DR CCDS; CCDS30315.1; -.
DR RefSeq; NP_062805.1; NM_019831.3.
DR RefSeq; XP_006528226.1; XM_006528163.3.
DR RefSeq; XP_006528227.1; XM_006528164.2.
DR RefSeq; XP_006528228.1; XM_006528165.3.
DR RefSeq; XP_006528229.1; XM_006528166.3.
DR AlphaFoldDB; Q9JLM4; -.
DR SMR; Q9JLM4; -.
DR BioGRID; 207927; 2.
DR IntAct; Q9JLM4; 1.
DR STRING; 10090.ENSMUSP00000068197; -.
DR iPTMnet; Q9JLM4; -.
DR PhosphoSitePlus; Q9JLM4; -.
DR EPD; Q9JLM4; -.
DR jPOST; Q9JLM4; -.
DR MaxQB; Q9JLM4; -.
DR PaxDb; Q9JLM4; -.
DR PRIDE; Q9JLM4; -.
DR ProteomicsDB; 299568; -.
DR Antibodypedia; 524; 180 antibodies from 24 providers.
DR DNASU; 56364; -.
DR Ensembl; ENSMUST00000063577; ENSMUSP00000068197; ENSMUSG00000031310.
DR GeneID; 56364; -.
DR KEGG; mmu:56364; -.
DR UCSC; uc009txm.2; mouse.
DR CTD; 9203; -.
DR MGI; MGI:1927231; Zmym3.
DR VEuPathDB; HostDB:ENSMUSG00000031310; -.
DR eggNOG; ENOG502QQQ9; Eukaryota.
DR GeneTree; ENSGT00940000160693; -.
DR InParanoid; Q9JLM4; -.
DR OMA; QKRFCNA; -.
DR OrthoDB; 587724at2759; -.
DR PhylomeDB; Q9JLM4; -.
DR TreeFam; TF336988; -.
DR BioGRID-ORCS; 56364; 5 hits in 75 CRISPR screens.
DR PRO; PR:Q9JLM4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9JLM4; protein.
DR Bgee; ENSMUSG00000031310; Expressed in embryonic brain and 250 other tissues.
DR ExpressionAtlas; Q9JLM4; baseline and differential.
DR Genevisible; Q9JLM4; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR InterPro; IPR021893; DUF3504.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR010507; Znf_MYM.
DR Pfam; PF12012; DUF3504; 1.
DR Pfam; PF06467; zf-FCS; 9.
DR SMART; SM00746; TRASH; 10.
PE 1: Evidence at protein level;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1370
FT /note="Zinc finger MYM-type protein 3"
FT /id="PRO_0000191379"
FT ZN_FING 334..368
FT /note="MYM-type 1"
FT ZN_FING 380..424
FT /note="MYM-type 2"
FT ZN_FING 431..466
FT /note="MYM-type 3"
FT ZN_FING 479..513
FT /note="MYM-type 4"
FT ZN_FING 523..561
FT /note="MYM-type 5"
FT ZN_FING 569..606
FT /note="MYM-type 6"
FT ZN_FING 614..648
FT /note="MYM-type 7"
FT ZN_FING 655..694
FT /note="MYM-type 8"
FT ZN_FING 701..735
FT /note="MYM-type 9"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..829
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 797
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT MOD_RES 818
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT MOD_RES 827
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CROSSLNK 322
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CROSSLNK 780
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CROSSLNK 788
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CROSSLNK 806
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CROSSLNK 848
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CROSSLNK 862
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CROSSLNK 921
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CROSSLNK 1276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14202"
FT CONFLICT 238..239
FT /note="Missing (in Ref. 2; BAC65550)"
FT /evidence="ECO:0000305"
FT CONFLICT 493..495
FT /note="KNT -> VGP (in Ref. 2; BAC65550)"
FT /evidence="ECO:0000305"
FT CONFLICT 719..735
FT /note="AARCHACKRQGKLLETI -> VRRVNRAERRQQGDELW (in Ref. 2;
FT BAC65550)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1370 AA; 152879 MW; E9270E68366E46F1 CRC64;
MDPSDFPSPF DPLTLPEKPL AGDLPVDMEF GEDLLESQTA PSRGWAPPGP SPSSGALDLL
DTPSGLEKDP GGVLDGATEL LGLGGLLYKA PSPPEVDHGP EGTLAWDSGE QTLEPGPGCQ
TPEVMPPDPG AGASPPSPEG LLEPLAPDSP IILESPHIEE EIPPLATRRR GSPGQEEEHT
QGQPQSPNAP PSPSVGETLG DGINSSQSKP GVCTPTAHPS LPGDGLTGKE IEKPPERVQK
RSERVRRAEP PKPEVVDSTE SIPVSDEDSD AMVDDPNDED FVPFRPRRSP RMSLRSSMAQ
RAGRSSMGTK MSCAHCRTPL QKGQTAYQRK GLPQLFCSSS CLTTYSKKPL GRKTCTFCKK
EIWNTKDSVV VQTGPGGSFH EFCTSVCLSL YEAQQQRPIP QSGDPADATR CSICQKTGEV
LHEVSNGSVV HRLCSDSCFS KFRANKGLKT NCCDQCGAYI YARPGGLGPE LLFHDGQQKR
FCNTTCLGAY KKKNTRVYPC VWCKTLCKNF EMLSHVDRNG KTSLFCSLCC TTSYKVKQAG
LTGPPRPCSF CRRSLSDPCY YNKVDRTVYQ FCSPSCWTKF QHTSPEGGIH LSCHYCHSLF
SGKPEVLEWQ DQVFQFCCRD CCEDFKRLRG VVSQCEHCRQ EKLLHEKLRF SGVEKSFCSE
GCVLLYKQDF TKKLGLCCIT CTYCSQTCQR GVTEQLDGST WDFCSEDCKT KYLLWYCKAA
RCHACKRQGK LLETIHWRGQ IRHFCNQQCL LRFYSQQNQP NLDTQSGPES LLNSQSSESK
PQTPSQTKVE NNHTVRTPDE NGNLGKTPVK RATPSVPTPP PPPPPATPRK NKAAMCKPLM
QNRGVSCKAE MKSKGSQTEE WKPQVIVLPI PVPIFVPVPM HLYCQKVPVP FSMPIPVPVP
MFLPTTLEST EKIVETIEEL KVKIPSNPLE ADILAMAEMI AEAEELDKAS SDLCDLVSNQ
SAEGLLEDCD LFGTARDDVL AMAVKMANVL DEPGQDLEAD FPKNPLDINP SVDFLFDCGL
VGPEDVSTEQ DLPRAMRKGQ KRLMLSESCS RDSLSSQPSC TGLNYSYGVN AWKCWVQSKY
ANGETSKGDE LRFGPKPMRI KEDILACSAA ELNYGLAQFV REITRPNGER YEPDSIYYLC
LGIQQYLLEN NRMVNIFTDL YYLTFVQELN KSLSTWQPTL LPNNTVFSRV EEEHLWECKQ
LGVYSPFVLL NTLMFFNTKF FGLQTAEEHM QLSFTNVVRQ SRKCTTPRGT TKVVSIRYYA
PVRQRKGRDT GPGKRKREDE TILEQRENRM NPLRCPVKFY EFYLSKCPES LRTRNDVFYL
QPERSCIAES PLWYSVIPMD RSMLESMLNR ILAVREIYEE LGRPGEEDLD
