GenomeNet

Database: UniProt
Entry: A0A0G2JWK2_RAT
LinkDB: A0A0G2JWK2_RAT
Original site: A0A0G2JWK2_RAT 
ID   A0A0G2JWK2_RAT          Unreviewed;       492 AA.
AC   A0A0G2JWK2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Methyl-CpG-binding protein 2 {ECO:0000256|PIRNR:PIRNR038006};
DE            Short=MeCp-2 protein {ECO:0000256|PIRNR:PIRNR038006};
DE            Short=MeCp2 {ECO:0000256|PIRNR:PIRNR038006};
GN   Name=Mecp2 {ECO:0000313|Ensembl:ENSRNOP00000069913.1,
GN   ECO:0000313|RGD:3075};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000069913.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000069913.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069913.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000069913.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069913.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Chromosomal protein that binds to methylated DNA. It can bind
CC       specifically to a single methyl-CpG pair. It is not influenced by
CC       sequences flanking the methyl-CpGs. Binds both 5-methylcytosine (5mC)
CC       and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference
CC       for 5-methylcytosine (5mC). {ECO:0000256|PIRNR:PIRNR038006}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038006}.
CC       Note=Colocalized with methyl-CpG in the genome.
CC       {ECO:0000256|PIRNR:PIRNR038006}.
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   RefSeq; NP_073164.2; NM_022673.2.
DR   RefSeq; XP_006229629.1; XM_006229567.3.
DR   AlphaFoldDB; A0A0G2JWK2; -.
DR   SMR; A0A0G2JWK2; -.
DR   Ensembl; ENSRNOT00000085723.2; ENSRNOP00000069913.1; ENSRNOG00000056659.2.
DR   GeneID; 29386; -.
DR   KEGG; rno:29386; -.
DR   CTD; 4204; -.
DR   RGD; 3075; Mecp2.
DR   GeneTree; ENSGT00530000063687; -.
DR   OrthoDB; 5262043at2759; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000056659; Expressed in skeletal muscle tissue and 18 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0010385; F:double-stranded methylated DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProtKB-UniRule.
DR   CDD; cd01396; MeCP2_MBD; 1.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR017353; Me_CpG-bd_MeCP2.
DR   InterPro; IPR045138; MeCP2/MBD4.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   PANTHER; PTHR15074; METHYL-CPG-BINDING PROTEIN; 1.
DR   PANTHER; PTHR15074:SF6; METHYL-CPG-BINDING PROTEIN 2; 1.
DR   Pfam; PF01429; MBD; 1.
DR   PIRSF; PIRSF038006; Methyl_CpG_bd_MeCP2; 1.
DR   SMART; SM00391; MBD; 1.
DR   SUPFAM; SSF54171; DNA-binding domain; 1.
DR   PROSITE; PS50982; MBD; 1.
PE   1: Evidence at protein level;
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR038006};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR038006};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JWK2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repressor {ECO:0000256|PIRNR:PIRNR038006};
KW   Transcription {ECO:0000256|PIRNR:PIRNR038006};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR038006}.
FT   DOMAIN          90..162
FT                   /note="MBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50982"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..398
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  53048 MW;  0B1EA5BBFE69EAAE CRC64;
     MVAGMLGLRE EKSEDQDLQG LKEKPLKFKK VKKDKKEDKE GKHEPLQPSA HHSAEPAEAG
     KAETSESSGS APAVPEASAS PKQRRSIIRD RGPMYDDPTL PEGWTRKLKQ RKSGRSAGKY
     DVYLINPQGK AFRSKVELIA YFEKVGDTSL DPNDFDFTVT GRGSPSRREQ KPPKKPKSPK
     APGTGRGRGR PKGSGTGRPK AAASEGVQVK RVLEKSPGKL LVKMPFQASP GGKGEGGGAT
     TSAQVMVIKR PGRKRKAEAD PQAIPKKRGR KPGSVVAAAA AEAKKKAVKE SSIRSVQETV
     LPIKKRKTRE TVSIEVKEVV KPLLVSTLGE KSGKGLKTCK SPGRKSKESS PKGRSSSASS
     PPKKEHHHHH HHAESPKAPM PLLPPPPPPE PQSSEDPISP PEPQDLSSSI CKEEKMPRAG
     SLESDGCPKE PAKTQPMVAA AATTTTTTTT TVAEKYKHRG EGERKDIVSS SMPRPNREEP
     VDSRTPVTER VS
//
DBGET integrated database retrieval system