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Database: UniProt
Entry: A0A2K5KX58_CERAT
LinkDB: A0A2K5KX58_CERAT
Original site: A0A2K5KX58_CERAT 
ID   A0A2K5KX58_CERAT        Unreviewed;       501 AA.
AC   A0A2K5KX58;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
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:ENSCATP00000005272.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000005272.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000005272.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
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DR   AlphaFoldDB; A0A2K5KX58; -.
DR   STRING; 9531.ENSCATP00000005272; -.
DR   Ensembl; ENSCATT00000020037.1; ENSCATP00000005272.1; ENSCATG00000017038.1.
DR   GeneTree; ENSGT00530000063687; -.
DR   OMA; PYKHERK; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000017038; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0010385; F:double-stranded methylated DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140566; F:histone reader activity; IEA:Ensembl.
DR   GO; GO:0008327; F:methyl-CpG binding; IEA:Ensembl.
DR   GO; GO:0140693; F:molecular condensate scaffold activity; IEA:Ensembl.
DR   GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR   GO; GO:0035197; F:siRNA binding; IEA:Ensembl.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR   GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR   GO; GO:0006576; P:biogenic amine metabolic process; IEA:Ensembl.
DR   GO; GO:0032048; P:cardiolipin metabolic process; IEA:Ensembl.
DR   GO; GO:0050432; P:catecholamine secretion; IEA:Ensembl.
DR   GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR   GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0071514; P:genomic imprinting; IEA:Ensembl.
DR   GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR   GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:Ensembl.
DR   GO; GO:0031507; P:heterochromatin formation; IEA:Ensembl.
DR   GO; GO:0006020; P:inositol metabolic process; IEA:Ensembl.
DR   GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProtKB-UniRule.
DR   GO; GO:0001976; P:nervous system process involved in regulation of systemic arterial blood pressure; IEA:Ensembl.
DR   GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:Ensembl.
DR   GO; GO:1905643; P:positive regulation of DNA methylation; IEA:Ensembl.
DR   GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
DR   GO; GO:0090063; P:positive regulation of microtubule nucleation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0019230; P:proprioception; IEA:Ensembl.
DR   GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR   GO; GO:0051570; P:regulation of histone H3-K9 methylation; IEA:Ensembl.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IEA:Ensembl.
DR   GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0051707; P:response to other organism; IEA:Ensembl.
DR   GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR   GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR   GO; GO:0001964; P:startle response; IEA:Ensembl.
DR   GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR   GO; GO:0099191; P:trans-synaptic signaling by BDNF; IEA:Ensembl.
DR   GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR   GO; GO:0008542; P:visual learning; IEA:Ensembl.
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   4: Predicted;
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR038006};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR038006};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   Repressor {ECO:0000256|PIRNR:PIRNR038006};
KW   Transcription {ECO:0000256|PIRNR:PIRNR038006};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR038006}.
FT   DOMAIN          105..177
FT                   /note="MBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50982"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..282
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..415
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  53772 MW;  628DA943E766C30A CRC64;
     DPPASASQSA GITGGSPRAR LAPQEEKSED QDLQGLKDKP LKFKKVKKDK KEDKEGKHEP
     VQPSAHHSAE PAEAGKAETS EGSGSAPAVP EASASPKQRR SIIRDRGPMY DDPTLPEGWT
     RKLKQRKSGR SAGKYDVYLI NPQGKAFRSK VELIAYFEKV GDTSLDPNDF DFTVTGRGSP
     SRREQKPPKK PKSPKAPGTG RGRGRPKGSG TTRPKAATSE GVQVKRVLEK SPGKLLVKMP
     FQTSPGGKAE GGGATTSTQV MVIKRPGRKR KAEADPQAIP KKRGRKPGSV VAAAAAEAKK
     KAVKESSIRS VQETVLPIKK RKTRETVSIE VKEVVKPLLV STLGEKSGKG LKTCKSPGRK
     SKESSPKGRS SSASSPPKKE HHHHHHHSES PKAPVPLLPP LPPPPPEPES SEDPTSPPEP
     QDLSSSVCKE EKMPRGGSLE SDGCPKEPAK TQPAVATAAT AAEKYKHRGE GERKDIVSSS
     MPRPNREEPV DSRTPVTERV S
//
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