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LMBL2_MOUSE
ID   LMBL2_MOUSE             Reviewed;         703 AA.
AC   P59178; Q8BHD5;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Lethal(3)malignant brain tumor-like protein 2;
DE            Short=L(3)mbt-like protein 2;
GN   Name=L3mbtl2;
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, PHOSPHORYLATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster;
RX   PubMed=14597177; DOI=10.1016/s0378-1119(03)00801-1;
RA   Markus J., Feikova S., Sramko M., Wolff L., Bies J.;
RT   "Proliferation-linked expression of the novel murine gene m4mbt encoding a
RT   nuclear zinc finger protein with four mbt domains.";
RL   Gene 319:117-126(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
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).
CC   -!- FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain
CC       the transcriptionally repressive state of genes, probably via a
CC       modification of chromatin, rendering it heritably changed in its
CC       expressibility. Its association with a chromatin-remodeling complex
CC       suggests that it may contribute to prevent expression of genes that
CC       trigger the cell into mitosis. Binds to monomethylated and dimethylated
CC       'Lys-20' on histone H4. Binds histone H3 peptides that are
CC       monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27' (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of the E2F6.com-1 complex in G0 phase composed of E2F6,
CC       MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, BAT8 and
CC       YAF2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14597177}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14597177}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:14597177}.
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DR   EMBL; AY237000; AAP44771.1; -; mRNA.
DR   EMBL; AK029115; BAC26305.1; -; mRNA.
DR   EMBL; AK036510; BAC29456.1; -; mRNA.
DR   EMBL; CH466550; EDL04569.1; -; Genomic_DNA.
DR   EMBL; BC023933; AAH23933.1; -; mRNA.
DR   EMBL; BC030864; AAH30864.1; -; mRNA.
DR   CCDS; CCDS27669.1; -.
DR   RefSeq; NP_666105.2; NM_145993.5.
DR   AlphaFoldDB; P59178; -.
DR   SMR; P59178; -.
DR   BioGRID; 229554; 53.
DR   IntAct; P59178; 14.
DR   MINT; P59178; -.
DR   STRING; 10090.ENSMUSP00000023029; -.
DR   iPTMnet; P59178; -.
DR   PhosphoSitePlus; P59178; -.
DR   MaxQB; P59178; -.
DR   PaxDb; P59178; -.
DR   PeptideAtlas; P59178; -.
DR   PRIDE; P59178; -.
DR   ProteomicsDB; 290041; -.
DR   Antibodypedia; 204; 219 antibodies from 27 providers.
DR   DNASU; 214669; -.
DR   Ensembl; ENSMUST00000023029; ENSMUSP00000023029; ENSMUSG00000022394.
DR   GeneID; 214669; -.
DR   KEGG; mmu:214669; -.
DR   UCSC; uc007wwu.2; mouse.
DR   CTD; 83746; -.
DR   MGI; MGI:2443584; L3mbtl2.
DR   VEuPathDB; HostDB:ENSMUSG00000022394; -.
DR   eggNOG; KOG3766; Eukaryota.
DR   GeneTree; ENSGT00940000153840; -.
DR   HOGENOM; CLU_005352_2_1_1; -.
DR   InParanoid; P59178; -.
DR   OMA; NYPGPSE; -.
DR   TreeFam; TF316498; -.
DR   Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR   BioGRID-ORCS; 214669; 6 hits in 74 CRISPR screens.
DR   ChiTaRS; L3mbtl2; mouse.
DR   PRO; PR:P59178; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P59178; protein.
DR   Bgee; ENSMUSG00000022394; Expressed in floor plate of midbrain and 221 other tissues.
DR   ExpressionAtlas; P59178; baseline and differential.
DR   Genevisible; P59178; MM.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; ISO:MGI.
DR   GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0031062; P:positive regulation of histone methylation; IMP:MGI.
DR   GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR   GO; GO:0072089; P:stem cell proliferation; IDA:MGI.
DR   Gene3D; 3.30.60.160; -; 1.
DR   InterPro; IPR038038; L3MBTL2.
DR   InterPro; IPR004092; Mbt.
DR   InterPro; IPR012313; Znf_FCS.
DR   InterPro; IPR038603; Znf_FCS_sf.
DR   PANTHER; PTHR12247:SF64; PTHR12247:SF64; 1.
DR   Pfam; PF02820; MBT; 4.
DR   SMART; SM00561; MBT; 4.
DR   PROSITE; PS51079; MBT; 4.
DR   PROSITE; PS51024; ZF_FCS; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..703
FT                   /note="Lethal(3)malignant brain tumor-like protein 2"
FT                   /id="PRO_0000084449"
FT   REPEAT          179..283
FT                   /note="MBT 1"
FT   REPEAT          291..391
FT                   /note="MBT 2"
FT   REPEAT          397..500
FT                   /note="MBT 3"
FT   REPEAT          508..604
FT                   /note="MBT 4"
FT   ZN_FING         81..116
FT                   /note="FCS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..637
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q969R5"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q969R5"
FT   MOD_RES         338
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q969R5"
FT   MOD_RES         681
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q969R5"
FT   MOD_RES         685
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3MIF2"
FT   MOD_RES         687
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q969R5"
FT   CROSSLNK        405
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q969R5"
FT   CROSSLNK        647
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q969R5"
FT   CROSSLNK        673
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q969R5"
FT   CROSSLNK        698
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q969R5"
FT   CROSSLNK        698
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q969R5"
FT   CONFLICT        682
FT                   /note="L -> P (in Ref. 4; AAH23933/AAH30864)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   703 AA;  78971 MW;  2E9B5DF5BFCEAFF9 CRC64;
     MEKPRGTEEA PSSEPMEEEE EDDLDLFGGY DSFRSYNSSA GSESSSYLEE SSEAENEDRE
     AGELPTSPLH LFSSANNRSL DGSGSEPAVC EMCGIVGTRE AFFSKTKRFC SVSCSRSYSS
     NSKKASILAR LQGKPPTKKA KVLHKAAWSA KIGAFLHAQG TGQLADGTPT GQDALVLGFD
     WGKFLKDHSY KAAPVSCFKH VPLYDQWEDV MKGMKVEVLN SDAVLPSRVY WIATVIQAAG
     YRVLLRYEGF ENDASHDFWC NLGTVDVHPI GWCAINSKIL VPPRTIHAKF TDWKSYLMKR
     LVGSRTLPAD FHIKMVESMK YPFRQGMRLE VVDKTQVSRT RMAVVDTVIG GRLRLLYEDG
     DSDDDFWCHM WSPLIHPVGW SRRVGHGIKM SDRRCDMSHH PTFRKIYCDA VPYLFKKVRA
     VYTEGGWFEE GMKLEAIDPL NLGSICVATI CKVLLDGYLM ICVDGGPSTD GSDWFCYHAS
     SHAIFPATFC QKNDIELTPP KGYETQPFAW ETYLEKTKSK AAPARLFNMD CPNHGFKVGM
     KLEAVDLMEP RLICVATVKR VVHRLLSIHF DGWDNEYDQW VDCESPDIYP VGWCELTGYQ
     LQPPVSAEPN TPQKGKDTTK KKKKQFGKKR KRIPSAKTRP LRQGSKKPLL EDNLEALGVS
     EPVPDDIIAV CVKEEHQDIS SLDRSPSPQL PLPIESIKQE RNN
 
 
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