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Methyl-CpG-binding domain protein 1 (Methyl-CpG-binding protein MBD1)

 MBD1_MOUSE              Reviewed;         636 AA.
Q9Z2E2; Q3TMA4; Q3U101; Q6NSW0; Q792D6; Q8CCL9; Q9DC19;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
24-JUL-2007, sequence version 2.
18-JUL-2018, entry version 145.
RecName: Full=Methyl-CpG-binding domain protein 1;
AltName: Full=Methyl-CpG-binding protein MBD1;
Name=Mbd1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=9774669; DOI=10.1128/MCB.18.11.6538;
Hendrich B., Bird A.;
"Identification and characterization of a family of mammalian methyl-
CpG binding proteins.";
Mol. Cell. Biol. 18:6538-6547(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129;
PubMed=10441743; DOI=10.1007/s003359901112;
Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.;
"Genomic structure and chromosomal mapping of the murine and human
mbd1, mbd2, mbd3, and mbd4 genes.";
Mamm. Genome 10:906-912(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
STRAIN=C57BL/6J, and NOD; TISSUE=Lung, Olfactory bulb, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION.
PubMed=12697822; DOI=10.1128/MCB.23.9.3226-3236.2003;
Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.;
"The methyl-CpG binding protein MBD1 interacts with the p150 subunit
of chromatin assembly factor 1.";
Mol. Cell. Biol. 23:3226-3236(2003).
[6]
FUNCTION, AND ALTERNATIVE SPLICING.
PubMed=15060159; DOI=10.1128/MCB.24.8.3387-3395.2004;
Joergensen H.F., Ben-Porath I., Bird A.P.;
"Mbd1 is recruited to both methylated and nonmethylated CpGs via
distinct DNA binding domains.";
Mol. Cell. Biol. 24:3387-3395(2004).
[7]
INTERACTION WITH TENM1, AND SUBCELLULAR LOCATION.
PubMed=15777793; DOI=10.1016/j.yexcr.2004.12.020;
Nunes S.M., Ferralli J., Choi K., Brown-Luedi M., Minet A.D.,
Chiquet-Ehrismann R.;
"The intracellular domain of teneurin-1 interacts with MBD1 and
CAP/ponsin resulting in subcellular codistribution and translocation
to the nuclear matrix.";
Exp. Cell Res. 305:122-132(2005).
-!- FUNCTION: Transcriptional repressor that binds CpG islands in
promoters where the DNA is methylated at position 5 of cytosine
within CpG dinucleotides. Binding is abolished by the presence of
7-mG that is produced by DNA damage by methylmethanesulfonate
(MMS). Acts as transcriptional repressor and plays a role in gene
silencing by recruiting AFT7IP, which in turn recruits factors
such as the histone methyltransferase SETDB1. Probably forms a
complex with SETDB1 and ATF7IP that represses transcription and
couples DNA methylation and histone 'Lys-9' trimethylation.
Isoform 1 can also repress transcription from unmethylated
promoters. {ECO:0000269|PubMed:15060159,
ECO:0000269|PubMed:9774669}.
-!- SUBUNIT: Interacts with OASL, AFT7IP, AFT7IP2 and BAHD1. Binds
CHAF1A and the SUV39H1-CBX5 complex via the MBD domain. Binds MGP
via the TRD domain. May be part of the MeCP1 complex. During DNA
replication, it recruits SETDB1 to form a S phase-specific complex
that facilitates methylation of H3 'Lys-9' during replication-
coupled chromatin assembly and is at least composed of the CAF-1
subunit CHAF1A, MBD1 and SETDB1 (By similarity). Isoform 2
interacts with the Ten-1 ICD form of TENM1. {ECO:0000250,
ECO:0000269|PubMed:15777793}.
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus matrix. Nucleus speckle.
Chromosome. Note=Nuclear, in a punctate pattern. Associated with
euchromatic regions of the chromosomes. Colocalizes with the Ten-1
ICD form of TENM1 in foci associated with the nuclear matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=MBD1a;
IsoId=Q9Z2E2-1; Sequence=Displayed;
Name=2; Synonyms=MBD1b;
IsoId=Q9Z2E2-2; Sequence=VSP_011072, VSP_011073;
Note=Ref.4 (AAH69837) sequence is in conflict in position:
144:S->F. {ECO:0000305};
Name=3; Synonyms=MBD1d;
IsoId=Q9Z2E2-3; Sequence=VSP_011072, VSP_011073, VSP_011074,
VSP_011075;
Name=4;
IsoId=Q9Z2E2-4; Sequence=VSP_011073;
Name=5;
IsoId=Q9Z2E2-5; Sequence=VSP_011073, VSP_011074, VSP_011075;
-!- TISSUE SPECIFICITY: Highly expressed in kidney, liver and brain.
Detected at lower levels in heart, lung, skeletal muscle, spleen
and testis. {ECO:0000269|PubMed:9774669}.
-!- DOMAIN: The methyl-CpG-binding domain (MBD) functions both in
binding to methylated DNA and in protein interactions.
{ECO:0000250}.
-!- DOMAIN: The third CXXC-type zinc finger mediates binding to non-
methylated CpG dinucleotides. {ECO:0000250}.
-!- DOMAIN: The transcriptional repression domain (TRD) is involved in
transcription repression and in protein interactions.
{ECO:0000250}.
-!- PTM: Sumoylated with SUMO1 by PIAS1 and PIAS3. Sumoylation affects
transcriptional silencing by preventing the interaction with
SETDB1. In contrast, sumoylation may increase interaction with
AFT7IP (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AF072240; AAC68869.1; -; mRNA.
EMBL; AF120978; AAD48908.1; -; Genomic_DNA.
EMBL; AK004624; BAB23419.1; -; mRNA.
EMBL; AK032535; BAC27914.1; -; mRNA.
EMBL; AK156401; BAE33700.1; -; mRNA.
EMBL; AK166042; BAE38538.1; -; mRNA.
EMBL; BC069837; AAH69837.1; -; mRNA.
CCDS; CCDS50321.1; -. [Q9Z2E2-2]
RefSeq; NP_038622.2; NM_013594.2.
UniGene; Mm.22522; -.
ProteinModelPortal; Q9Z2E2; -.
SMR; Q9Z2E2; -.
BioGrid; 201330; 1.
IntAct; Q9Z2E2; 1.
MINT; Q9Z2E2; -.
iPTMnet; Q9Z2E2; -.
PhosphoSitePlus; Q9Z2E2; -.
PeptideAtlas; Q9Z2E2; -.
PRIDE; Q9Z2E2; -.
GeneID; 17190; -.
KEGG; mmu:17190; -.
UCSC; uc008fpj.2; mouse. [Q9Z2E2-2]
UCSC; uc008fpk.1; mouse. [Q9Z2E2-5]
UCSC; uc012bex.1; mouse. [Q9Z2E2-1]
CTD; 4152; -.
MGI; MGI:1333811; Mbd1.
HOVERGEN; HBG052416; -.
InParanoid; Q9Z2E2; -.
KO; K11589; -.
PhylomeDB; Q9Z2E2; -.
TreeFam; TF350557; -.
PRO; PR:Q9Z2E2; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MBD1; -.
GO; GO:0000785; C:chromatin; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0000792; C:heterochromatin; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0010385; F:double-stranded methylated DNA binding; ISO:MGI.
GO; GO:0008327; F:methyl-CpG binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016177; DNA-bd_dom_sf.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
InterPro; IPR002857; Znf_CXXC.
Pfam; PF01429; MBD; 1.
Pfam; PF02008; zf-CXXC; 3.
SMART; SM00391; MBD; 1.
SUPFAM; SSF54171; SSF54171; 1.
PROSITE; PS50982; MBD; 1.
PROSITE; PS51058; ZF_CXXC; 3.
1: Evidence at protein level;
Alternative splicing; Chromosome; Complete proteome; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 636 Methyl-CpG-binding domain protein 1.
/FTId=PRO_0000096259.
DOMAIN 1 69 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
ZN_FING 187 234 CXXC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
ZN_FING 235 281 CXXC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
ZN_FING 348 396 CXXC-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
REGION 550 612 TRD.
MOTIF 84 88 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIS9}.
CROSSLNK 117 117 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIS9}.
CROSSLNK 293 293 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIS9}.
CROSSLNK 443 443 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIS9}.
CROSSLNK 461 461 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIS9}.
CROSSLNK 520 520 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 520 520 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q9UIS9}.
CROSSLNK 559 559 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 559 559 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q9UIS9}.
VAR_SEQ 142 142 S -> SSSASASAS (in isoform 2 and isoform
3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_011072.
VAR_SEQ 345 400 Missing (in isoform 2, isoform 3, isoform
4 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_011073.
VAR_SEQ 614 625 LHKLLAVNEKEY -> SKDLKNPEAKMQ (in isoform
3 and isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_011074.
VAR_SEQ 626 636 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_011075.
CONFLICT 109 109 I -> R (in Ref. 3; BAB23419 and 4;
AAH69837). {ECO:0000305}.
CONFLICT 146 146 H -> R (in Ref. 4; AAH69837).
{ECO:0000305}.
CONFLICT 457 457 R -> Q (in Ref. 1; AAC68869, 2; AAD48908
and 3; BAE33700). {ECO:0000305}.
CONFLICT 484 484 T -> A (in Ref. 1; AAC68869, 2; AAD48908
and 3; BAE33700). {ECO:0000305}.
CONFLICT 497 497 S -> C (in Ref. 1; AAC68869, 2; AAD48908
and 3; BAE33700). {ECO:0000305}.
CONFLICT 556 556 S -> P (in Ref. 1; AAC68869, 2; AAD48908
and 3; BAE33700). {ECO:0000305}.
CONFLICT 604 604 L -> F (in Ref. 4; AAH69837).
{ECO:0000305}.
SEQUENCE 636 AA; 70023 MW; 02D8B94EBD522F65 CRC64;
MAESWQDCPA LGPGWKRRES FRKSGASFGR SDIYYQSPTG EKIRSKVELT RYLGPACDLT
LFDFRQGTLC HPIPKTHPLA VPSKKKKKPS KPAKTKKQQV GLQRSEVRIE TPQGEYKAPT
ATALASLSVS ASASSSASAS ASASSHAPVC CENCGIHFSW DGVKRQRLKT LCKDCRAQRI
AFNREQRMFK RVGCGDCAAC LVKEDCGVCS TCRLQLPSDV ASGLYCKCER RRCLRIMEKS
RGCGVCRGCQ TQEDCGHCCI CLRSPRPGLK RQWRCLQRRC FWGKRDSSKR GSKVASQRHS
QAPPLPPHPA SQYTEPTELH ISDIAPTSPA EFIYYCVDED EDELQPYTNQ RQNRKCGACA
ACLRRMDCGR CDFCCDKPKF GGGNQKRQKC RWRQCLQFAM KRLLPSAGSG SGEGAGLRPY
QTHQTHQKRP ASARQLQLSS PLKAPWAVVT APPGPVRDSR KQQAGRGSVL PQPDTDFVFL
QEGTSSAMQM PGTAAASTEV PVQAAQCSAP SWVVALPQVK QETADAPEEW TAVTTFLTSS
TLQSGFPSKA ADPDLSPVKQ EPPGPEEDGE EKKDDVSETT PAEEIGGVGT PVITEIFSLG
GTRLRDAEAW LPRLHKLLAV NEKEYFTELQ LKEEVL


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