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Q9UIS9

- MBD1_HUMAN

UniProt

Q9UIS9 - MBD1_HUMAN

Protein

Methyl-CpG-binding domain protein 1

Gene

MBD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    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 and isoform 2 can also repress transcription from unmethylated promoters.10 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri169 – 21648CXXC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri217 – 26347CXXC-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri330 – 37849CXXC-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. methyl-CpG binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. sequence-specific DNA binding transcription factor activity Source: ProtInc
    5. transcription corepressor activity Source: ProtInc
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. negative regulation of transcription, DNA-templated Source: UniProtKB
    2. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-CpG-binding domain protein 1
    Alternative name(s):
    CXXC-type zinc finger protein 3
    Methyl-CpG-binding protein MBD1
    Protein containing methyl-CpG-binding domain 1
    Gene namesi
    Name:MBD1
    Synonyms:CXXC3, PCM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:6916. MBD1.

    Subcellular locationi

    Nucleus By similarity. Nucleus matrix By similarity. Nucleus speckle. Chromosome
    Note: Colocalizes with the Ten-1 ICD form of TENM1 in foci associated with the nuclear matrix By similarity. Nuclear, in a punctate pattern. Associated with euchromatic regions of the chromosomes, with pericentromeric regions on chromosome 1 and with telomeric regions from several chromosomes.By similarity

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. nuclear matrix Source: UniProtKB
    3. nuclear speck Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 221R → A: Abolishes binding to methylated DNA.
    Mutagenesisi30 – 301R → A: Strongly reduces binding to methylated DNA. 1 Publication
    Mutagenesisi32 – 321D → A: Strongly reduces binding to methylated DNA. 1 Publication
    Mutagenesisi34 – 341Y → A: Reduces binding to methylated DNA. 1 Publication
    Mutagenesisi44 – 441R → A: Abolishes binding to methylated DNA. 1 Publication
    Mutagenesisi45 – 451S → A: Slightly reduces binding to methylated DNA. 1 Publication
    Mutagenesisi52 – 521Y → A: No effect. 1 Publication
    Mutagenesisi64 – 641F → A: Disrupts tertiary structure and abolishes DNA binding. 1 Publication
    Mutagenesisi499 – 4991K → A: Abolishes sumoylation; when associated with A-538. 1 Publication
    Mutagenesisi501 – 5011E → A: Abolishes sumoylation; when associated with A-540. 1 Publication
    Mutagenesisi538 – 5381K → A: Abolishes sumoylation; when associated with A-499. 1 Publication
    Mutagenesisi540 – 5401E → A: Abolishes sumoylation; when associated with A-501. 1 Publication
    Mutagenesisi576 – 5761I → R: Abolishes interaction with AFT7IP and subsequent transcription repression activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA30659.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 605605Methyl-CpG-binding domain protein 1PRO_0000096258Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei399 – 3991Phosphoserine3 Publications
    Cross-linki499 – 499Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki538 – 538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    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.2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UIS9.
    PaxDbiQ9UIS9.
    PRIDEiQ9UIS9.

    PTM databases

    PhosphoSiteiQ9UIS9.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Inductioni

    Up-regulated by interferon.1 Publication

    Gene expression databases

    ArrayExpressiQ9UIS9.
    BgeeiQ9UIS9.
    CleanExiHS_PCM1.
    GenevestigatoriQ9UIS9.

    Organism-specific databases

    HPAiCAB009017.
    CAB036003.

    Interactioni

    Subunit structurei

    Interacts with the Ten-1 ICD form of TENM1 By similarity. 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 similarity12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBX5P459736EBI-867196,EBI-78219
    CHAF1AQ131113EBI-867196,EBI-1020839
    HDAC1Q135472EBI-867196,EBI-301834
    HDAC2Q927692EBI-867196,EBI-301821
    HDAC3O153793EBI-867196,EBI-607682
    HTTP428582EBI-867196,EBI-466029
    PIAS1O759253EBI-867196,EBI-629434
    PIAS3Q9Y6X23EBI-867196,EBI-2803703
    PML-RARQ151564EBI-867196,EBI-867256
    SETDB1Q150473EBI-867196,EBI-79691
    SUMO1P631653EBI-867196,EBI-80140
    SUV39H1O434635EBI-867196,EBI-349968

    Protein-protein interaction databases

    BioGridi110322. 26 interactions.
    IntActiQ9UIS9. 14 interactions.
    MINTiMINT-2860643.

    Structurei

    Secondary structure

    1
    605
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Turni9 – 113
    Beta strandi16 – 194
    Beta strandi21 – 255
    Beta strandi33 – 364
    Beta strandi38 – 403
    Helixi47 – 537
    Beta strandi55 – 573
    Turni64 – 663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D9NNMR-A1-75[»]
    1IG4NMR-A1-75[»]
    ProteinModelPortaliQ9UIS9.
    SMRiQ9UIS9. Positions 1-75, 336-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UIS9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6969MBDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni529 – 59264TRDAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi84 – 885Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi284 – 31330Pro-richAdd
    BLAST

    Domaini

    The methyl-CpG-binding domain (MBD) functions both in binding to methylated DNA and in protein interactions.
    The third CXXC-type zinc finger mediates binding to non-methylated CpG dinucleotides.
    The transcriptional repression domain (TRD) is involved in transcription repression and in protein interactions.

    Sequence similaritiesi

    Contains 3 CXXC-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri169 – 21648CXXC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri217 – 26347CXXC-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri330 – 37849CXXC-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG145219.
    HOVERGENiHBG052416.
    InParanoidiQ9UIS9.
    KOiK11589.
    OrthoDBiEOG7QNVMV.
    PhylomeDBiQ9UIS9.

    Family and domain databases

    Gene3Di3.30.890.10. 1 hit.
    InterProiIPR016177. DNA-bd_dom.
    IPR001739. Methyl_CpG_DNA-bd.
    IPR002857. Znf_CXXC.
    [Graphical view]
    PfamiPF01429. MBD. 1 hit.
    PF02008. zf-CXXC. 3 hits.
    [Graphical view]
    SMARTiSM00391. MBD. 1 hit.
    [Graphical view]
    SUPFAMiSSF54171. SSF54171. 1 hit.
    PROSITEiPS50982. MBD. 1 hit.
    PS51058. ZF_CXXC. 3 hits.
    [Graphical view]

    Sequences (11)i

    Sequence statusi: Complete.

    This entry describes 11 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UIS9-1) [UniParc]FASTAAdd to Basket

    Also known as: MBD1v1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT    50
    RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV 100
    GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL 150
    KTLCKDCRAQ RIAFNREQRM FKRVGCGECA ACQVTEDCGA CSTCLLQLPH 200
    DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC PICLRPPRPG 250
    LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP 300
    TEPHPRALAP SPPAEFIYYC VDEDELQPYT NRRQNRKCGA CAACLRRMDC 350
    GRCDFCCDKP KFGGSNQKRQ KCRWRQCLQF AMKRLLPSVW SESEDGAGSP 400
    PPYRRRKRPS SARRHHLGPT LKPTLATRTA QPDHTQAPTK QEAGGGFVLP 450
    PPGTDLVFLR EGASSPVQVP GPVAASTEAL LQEAQCSGLS WVVALPQVKQ 500
    EKADTQDEWT PGTAVLTSPV LVPGCPSKAV DPGLPSVKQE PPDPEEDKEE 550
    NKDDSASKLA PEEEAGGAGT PVITEIFSLG GTRFRDTAVW LPRSKDLKKP 600
    GARKQ 605
    Length:605
    Mass (Da):66,607
    Last modified:July 19, 2004 - v2
    Checksum:i665732782CC6A32A
    GO
    Isoform 2 (identifier: Q9UIS9-2) [UniParc]FASTAAdd to Basket

    Also known as: MBD1v2

    The sequence of this isoform differs from the canonical sequence as follows:
         304-326: Missing.
         483-528: Missing.
         593-605: RSKDLKKPGARKQ → SLQGRHSGRE...RRSWCPSSQS

    Show »
    Length:586
    Mass (Da):64,677
    Checksum:iB77C386F65EA8718
    GO
    Isoform 4 (identifier: Q9UIS9-4) [UniParc]FASTAAdd to Basket

    Also known as: MBD1v3

    The sequence of this isoform differs from the canonical sequence as follows:
         327-382: Missing.
         483-528: Missing.

    Show »
    Length:503
    Mass (Da):55,167
    Checksum:iC5D0267B1D464ACD
    GO
    Isoform 5 (identifier: Q9UIS9-5) [UniParc]FASTAAdd to Basket

    Also known as: PCM1

    The sequence of this isoform differs from the canonical sequence as follows:
         173-221: Missing.

    Show »
    Length:556
    Mass (Da):61,265
    Checksum:i2426F8B3EFD49E3B
    GO
    Isoform 6 (identifier: Q9UIS9-6) [UniParc]FASTAAdd to Basket

    Also known as: MBD1v6

    The sequence of this isoform differs from the canonical sequence as follows:
         483-528: Missing.
         573-596: ITEIFSLGGTRFRDTAVWLPRSKD → EPTTQPQYSGNFDNDLYEIYLIDI
         597-605: Missing.

    Show »
    Length:550
    Mass (Da):60,848
    Checksum:i34194D340ED94FAB
    GO
    Isoform 7 (identifier: Q9UIS9-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         327-382: Missing.

    Show »
    Length:549
    Mass (Da):60,001
    Checksum:i45456E4E96182B5C
    GO
    Isoform 8 (identifier: Q9UIS9-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         304-326: Missing.
         483-528: Missing.

    Show »
    Length:536
    Mass (Da):59,158
    Checksum:i9ED6B5AEF1FF8BD9
    GO
    Isoform 9 (identifier: Q9UIS9-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         264-264: R → RHLAHRLRRRHQRCQRRTPLAVAPPT

    Show »
    Length:630
    Mass (Da):69,617
    Checksum:i23AF6E138EA8AD82
    GO
    Isoform 10 (identifier: Q9UIS9-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         173-221: Missing.
         327-327: Missing.
         594-605: SKDLKKPGARKQ → YYHLALDWKCNCGYHLCCRSVLVP

    Note: No experimental confirmation available.

    Show »
    Length:567
    Mass (Da):62,639
    Checksum:i1C2991C7EEE79687
    GO
    Isoform 11 (identifier: Q9UIS9-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         326-382: LQPYTNRRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGSNQKRQKCRWRQCLQFAM → L
         483-528: Missing.
         594-605: SKDLKKPGARKQ → AGTREGKMDVKCGRPRTQWSPRARAGTHEDGLEPMSVSHHLQLR

    Note: No experimental confirmation available.

    Show »
    Length:535
    Mass (Da):58,752
    Checksum:iBC13139056A0875D
    GO
    Isoform 12 (identifier: Q9UIS9-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         593-605: RSKDLKKPGARKQ → SLQGRHSGRE...RRSWCPSSQS

    Note: No experimental confirmation available.

    Show »
    Length:655
    Mass (Da):72,126
    Checksum:i0B83174575D7A4BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti239 – 2391H → R in ABP02056. 1 PublicationCurated
    Sequence conflicti330 – 3301T → M in ABP02056. 1 PublicationCurated
    Sequence conflicti348 – 3492MD → NG in CAA71735. (PubMed:9207790)Curated
    Sequence conflicti348 – 3492MD → NG in AAD51442. (PubMed:10454587)Curated
    Sequence conflicti348 – 3492MD → NG in AAD51443. (PubMed:10454587)Curated
    Sequence conflicti489 – 4891L → M in CAA71735. (PubMed:9207790)Curated
    Isoform 7 (identifier: Q9UIS9-7)
    Sequence conflicti327 – 3271K → Q in AAD51444. (PubMed:10454587)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti401 – 4011P → A.1 Publication
    Corresponds to variant rs125555 [ dbSNP | Ensembl ].
    VAR_019513

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei173 – 22149Missing in isoform 5 and isoform 10. 1 PublicationVSP_011064Add
    BLAST
    Alternative sequencei264 – 2641R → RHLAHRLRRRHQRCQRRTPL AVAPPT in isoform 9. 1 PublicationVSP_042812
    Alternative sequencei304 – 32623Missing in isoform 2 and isoform 8. 2 PublicationsVSP_011065Add
    BLAST
    Alternative sequencei326 – 38257LQPYT…LQFAM → L in isoform 11. CuratedVSP_054736Add
    BLAST
    Alternative sequencei327 – 38256Missing in isoform 4 and isoform 7. 2 PublicationsVSP_011066Add
    BLAST
    Alternative sequencei327 – 3271Missing in isoform 10. CuratedVSP_054737
    Alternative sequencei483 – 52846Missing in isoform 2, isoform 4, isoform 6, isoform 8 and isoform 11. 2 PublicationsVSP_011068Add
    BLAST
    Alternative sequencei573 – 59624ITEIF…PRSKD → EPTTQPQYSGNFDNDLYEIY LIDI in isoform 6. CuratedVSP_011069Add
    BLAST
    Alternative sequencei593 – 60513RSKDL…GARKQ → SLQGRHSGREDGCKVWETED TVEPTSTSWNPRGWPGTHVS LSPPPASMMWVSCRRSWCPS SQS in isoform 2 and isoform 12. 1 PublicationVSP_011070Add
    BLAST
    Alternative sequencei594 – 60512SKDLK…GARKQ → YYHLALDWKCNCGYHLCCRS VLVP in isoform 10. CuratedVSP_054738Add
    BLAST
    Alternative sequencei594 – 60512SKDLK…GARKQ → AGTREGKMDVKCGRPRTQWS PRARAGTHEDGLEPMSVSHH LQLR in isoform 11. CuratedVSP_054739Add
    BLAST
    Alternative sequencei597 – 6059Missing in isoform 6. CuratedVSP_011071

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10746 mRNA. Translation: CAA71735.1.
    AF120981, AF120980 Genomic DNA. Translation: AAD50371.1.
    AF078830 mRNA. Translation: AAD51442.1.
    AF078831 mRNA. Translation: AAD51443.1.
    AF078832 mRNA. Translation: AAD51444.1.
    AF078833 mRNA. Translation: AAD51445.1.
    EF488685 mRNA. Translation: ABP02056.1.
    AK302004 mRNA. Translation: BAG63407.1.
    AC090246 Genomic DNA. No translation available.
    BC033242 mRNA. Translation: AAH33242.1.
    AJ564845 mRNA. Translation: CAD92308.1.
    AF072241 mRNA. Translation: AAC68870.1.
    CCDSiCCDS11941.1. [Q9UIS9-4]
    CCDS11942.1. [Q9UIS9-7]
    CCDS11943.1. [Q9UIS9-1]
    CCDS11944.1. [Q9UIS9-5]
    CCDS32832.1. [Q9UIS9-2]
    CCDS56071.1. [Q9UIS9-8]
    CCDS56072.1. [Q9UIS9-6]
    CCDS56073.1. [Q9UIS9-9]
    CCDS59318.1. [Q9UIS9-10]
    CCDS59319.1. [Q9UIS9-11]
    CCDS59320.1. [Q9UIS9-12]
    RefSeqiNP_001191065.1. NM_001204136.1. [Q9UIS9-12]
    NP_001191066.1. NM_001204137.1. [Q9UIS9-9]
    NP_001191067.1. NM_001204138.1.
    NP_001191068.1. NM_001204139.1. [Q9UIS9-1]
    NP_001191069.1. NM_001204140.1.
    NP_001191070.1. NM_001204141.1. [Q9UIS9-10]
    NP_001191071.1. NM_001204142.1. [Q9UIS9-6]
    NP_001191072.1. NM_001204143.1. [Q9UIS9-11]
    NP_001191080.1. NM_001204151.1. [Q9UIS9-8]
    NP_002375.1. NM_002384.2. [Q9UIS9-4]
    NP_056669.2. NM_015844.2. [Q9UIS9-7]
    NP_056670.2. NM_015845.3. [Q9UIS9-2]
    NP_056671.2. NM_015846.3. [Q9UIS9-1]
    NP_056723.2. NM_015847.3. [Q9UIS9-5]
    XP_005258328.1. XM_005258271.1. [Q9UIS9-1]
    XP_006722534.1. XM_006722471.1. [Q9UIS9-7]
    XP_006722535.1. XM_006722472.1. [Q9UIS9-4]
    UniGeneiHs.405610.

    Genome annotation databases

    EnsembliENST00000269468; ENSP00000269468; ENSG00000141644. [Q9UIS9-1]
    ENST00000269471; ENSP00000269471; ENSG00000141644. [Q9UIS9-2]
    ENST00000339998; ENSP00000339546; ENSG00000141644. [Q9UIS9-6]
    ENST00000347968; ENSP00000285102; ENSG00000141644. [Q9UIS9-7]
    ENST00000353909; ENSP00000269469; ENSG00000141644. [Q9UIS9-5]
    ENST00000382948; ENSP00000372407; ENSG00000141644. [Q9UIS9-1]
    ENST00000398488; ENSP00000381502; ENSG00000141644. [Q9UIS9-4]
    ENST00000398493; ENSP00000381506; ENSG00000141644. [Q9UIS9-7]
    ENST00000457839; ENSP00000405268; ENSG00000141644. [Q9UIS9-9]
    ENST00000585595; ENSP00000468430; ENSG00000141644. [Q9UIS9-9]
    ENST00000585672; ENSP00000466092; ENSG00000141644. [Q9UIS9-10]
    ENST00000587605; ENSP00000468042; ENSG00000141644. [Q9UIS9-11]
    ENST00000588937; ENSP00000467763; ENSG00000141644. [Q9UIS9-2]
    ENST00000590208; ENSP00000468785; ENSG00000141644. [Q9UIS9-12]
    ENST00000591416; ENSP00000467017; ENSG00000141644. [Q9UIS9-1]
    ENST00000591535; ENSP00000465923; ENSG00000141644. [Q9UIS9-8]
    GeneIDi4152.
    KEGGihsa:4152.
    UCSCiuc002leg.3. human. [Q9UIS9-5]
    uc002leh.4. human. [Q9UIS9-7]
    uc002lei.4. human. [Q9UIS9-1]
    uc002lej.4. human. [Q9UIS9-4]
    uc002lel.4. human. [Q9UIS9-2]
    uc002len.3. human. [Q9UIS9-6]
    uc010dox.1. human. [Q9UIS9-8]
    uc010xdk.2. human. [Q9UIS9-9]

    Polymorphism databases

    DMDMi50401200.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10746 mRNA. Translation: CAA71735.1 .
    AF120981 , AF120980 Genomic DNA. Translation: AAD50371.1 .
    AF078830 mRNA. Translation: AAD51442.1 .
    AF078831 mRNA. Translation: AAD51443.1 .
    AF078832 mRNA. Translation: AAD51444.1 .
    AF078833 mRNA. Translation: AAD51445.1 .
    EF488685 mRNA. Translation: ABP02056.1 .
    AK302004 mRNA. Translation: BAG63407.1 .
    AC090246 Genomic DNA. No translation available.
    BC033242 mRNA. Translation: AAH33242.1 .
    AJ564845 mRNA. Translation: CAD92308.1 .
    AF072241 mRNA. Translation: AAC68870.1 .
    CCDSi CCDS11941.1. [Q9UIS9-4 ]
    CCDS11942.1. [Q9UIS9-7 ]
    CCDS11943.1. [Q9UIS9-1 ]
    CCDS11944.1. [Q9UIS9-5 ]
    CCDS32832.1. [Q9UIS9-2 ]
    CCDS56071.1. [Q9UIS9-8 ]
    CCDS56072.1. [Q9UIS9-6 ]
    CCDS56073.1. [Q9UIS9-9 ]
    CCDS59318.1. [Q9UIS9-10 ]
    CCDS59319.1. [Q9UIS9-11 ]
    CCDS59320.1. [Q9UIS9-12 ]
    RefSeqi NP_001191065.1. NM_001204136.1. [Q9UIS9-12 ]
    NP_001191066.1. NM_001204137.1. [Q9UIS9-9 ]
    NP_001191067.1. NM_001204138.1.
    NP_001191068.1. NM_001204139.1. [Q9UIS9-1 ]
    NP_001191069.1. NM_001204140.1.
    NP_001191070.1. NM_001204141.1. [Q9UIS9-10 ]
    NP_001191071.1. NM_001204142.1. [Q9UIS9-6 ]
    NP_001191072.1. NM_001204143.1. [Q9UIS9-11 ]
    NP_001191080.1. NM_001204151.1. [Q9UIS9-8 ]
    NP_002375.1. NM_002384.2. [Q9UIS9-4 ]
    NP_056669.2. NM_015844.2. [Q9UIS9-7 ]
    NP_056670.2. NM_015845.3. [Q9UIS9-2 ]
    NP_056671.2. NM_015846.3. [Q9UIS9-1 ]
    NP_056723.2. NM_015847.3. [Q9UIS9-5 ]
    XP_005258328.1. XM_005258271.1. [Q9UIS9-1 ]
    XP_006722534.1. XM_006722471.1. [Q9UIS9-7 ]
    XP_006722535.1. XM_006722472.1. [Q9UIS9-4 ]
    UniGenei Hs.405610.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D9N NMR - A 1-75 [» ]
    1IG4 NMR - A 1-75 [» ]
    ProteinModelPortali Q9UIS9.
    SMRi Q9UIS9. Positions 1-75, 336-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110322. 26 interactions.
    IntActi Q9UIS9. 14 interactions.
    MINTi MINT-2860643.

    PTM databases

    PhosphoSitei Q9UIS9.

    Polymorphism databases

    DMDMi 50401200.

    Proteomic databases

    MaxQBi Q9UIS9.
    PaxDbi Q9UIS9.
    PRIDEi Q9UIS9.

    Protocols and materials databases

    DNASUi 4152.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269468 ; ENSP00000269468 ; ENSG00000141644 . [Q9UIS9-1 ]
    ENST00000269471 ; ENSP00000269471 ; ENSG00000141644 . [Q9UIS9-2 ]
    ENST00000339998 ; ENSP00000339546 ; ENSG00000141644 . [Q9UIS9-6 ]
    ENST00000347968 ; ENSP00000285102 ; ENSG00000141644 . [Q9UIS9-7 ]
    ENST00000353909 ; ENSP00000269469 ; ENSG00000141644 . [Q9UIS9-5 ]
    ENST00000382948 ; ENSP00000372407 ; ENSG00000141644 . [Q9UIS9-1 ]
    ENST00000398488 ; ENSP00000381502 ; ENSG00000141644 . [Q9UIS9-4 ]
    ENST00000398493 ; ENSP00000381506 ; ENSG00000141644 . [Q9UIS9-7 ]
    ENST00000457839 ; ENSP00000405268 ; ENSG00000141644 . [Q9UIS9-9 ]
    ENST00000585595 ; ENSP00000468430 ; ENSG00000141644 . [Q9UIS9-9 ]
    ENST00000585672 ; ENSP00000466092 ; ENSG00000141644 . [Q9UIS9-10 ]
    ENST00000587605 ; ENSP00000468042 ; ENSG00000141644 . [Q9UIS9-11 ]
    ENST00000588937 ; ENSP00000467763 ; ENSG00000141644 . [Q9UIS9-2 ]
    ENST00000590208 ; ENSP00000468785 ; ENSG00000141644 . [Q9UIS9-12 ]
    ENST00000591416 ; ENSP00000467017 ; ENSG00000141644 . [Q9UIS9-1 ]
    ENST00000591535 ; ENSP00000465923 ; ENSG00000141644 . [Q9UIS9-8 ]
    GeneIDi 4152.
    KEGGi hsa:4152.
    UCSCi uc002leg.3. human. [Q9UIS9-5 ]
    uc002leh.4. human. [Q9UIS9-7 ]
    uc002lei.4. human. [Q9UIS9-1 ]
    uc002lej.4. human. [Q9UIS9-4 ]
    uc002lel.4. human. [Q9UIS9-2 ]
    uc002len.3. human. [Q9UIS9-6 ]
    uc010dox.1. human. [Q9UIS9-8 ]
    uc010xdk.2. human. [Q9UIS9-9 ]

    Organism-specific databases

    CTDi 4152.
    GeneCardsi GC18M047795.
    HGNCi HGNC:6916. MBD1.
    HPAi CAB009017.
    CAB036003.
    MIMi 156535. gene.
    neXtProti NX_Q9UIS9.
    PharmGKBi PA30659.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145219.
    HOVERGENi HBG052416.
    InParanoidi Q9UIS9.
    KOi K11589.
    OrthoDBi EOG7QNVMV.
    PhylomeDBi Q9UIS9.

    Miscellaneous databases

    EvolutionaryTracei Q9UIS9.
    GeneWikii MBD1.
    GenomeRNAii 4152.
    NextBioi 16330.
    PROi Q9UIS9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UIS9.
    Bgeei Q9UIS9.
    CleanExi HS_PCM1.
    Genevestigatori Q9UIS9.

    Family and domain databases

    Gene3Di 3.30.890.10. 1 hit.
    InterProi IPR016177. DNA-bd_dom.
    IPR001739. Methyl_CpG_DNA-bd.
    IPR002857. Znf_CXXC.
    [Graphical view ]
    Pfami PF01429. MBD. 1 hit.
    PF02008. zf-CXXC. 3 hits.
    [Graphical view ]
    SMARTi SM00391. MBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54171. SSF54171. 1 hit.
    PROSITEi PS50982. MBD. 1 hit.
    PS51058. ZF_CXXC. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins."
      Cross S.H., Meehan R.R., Nan X., Bird A.
      Nat. Genet. 16:256-259(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH THE MECP1 COMPLEX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Genomic structure and chromosomal mapping of the murine and human mbd1, mbd2, mbd3, and mbd4 genes."
      Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.
      Mamm. Genome 10:906-912(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-401.
    3. "Methylation-mediated transcriptional silencing in euchromatin by methyl-CpG binding protein MBD1 isoforms."
      Fujita N., Takebayashi S., Okumura K., Kudo S., Chiba T., Saya H., Nakao M.
      Mol. Cell. Biol. 19:6415-6426(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 7), FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Fibroblast.
    4. "Interaction between the 2'-5' oligoadenylate synthetase-like protein p59 OASL and the transcriptional repressor methyl CpG-binding protein 1."
      Andersen J.B., Strandbygaard D.J., Hartmann R., Justesen J.
      Eur. J. Biochem. 271:628-636(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 6), INDUCTION BY INTERFERON, INTERACTION WITH OASL.
      Tissue: Leukocyte.
    5. "New splice variant of the methyl-CpG binding protein 1 (MBD1)."
      Laget S.M., Xu S.-Y.
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
      Tissue: Cervix carcinoma.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
      Tissue: Prostate.
    9. "Identification and characterization of a family of mammalian methyl-CpG binding proteins."
      Hendrich B., Bird A.
      Mol. Cell. Biol. 18:6538-6547(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 169-220, FUNCTION.
    10. "Active repression of methylated genes by the chromosomal protein MBD1."
      Ng H.-H., Jeppesen P., Bird A.
      Mol. Cell. Biol. 20:1394-1406(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression."
      Fujita N., Watanabe S., Ichimura T., Tsuruzoe S., Shinkai Y., Tachibana M., Chiba T., Nakao M.
      J. Biol. Chem. 278:24132-24138(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE SUV39H1-CBX5 COMPLEX.
    12. Cited for: FUNCTION, INTERACTION WITH AFT7IP.
    13. "The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1."
      Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.
      Mol. Cell. Biol. 23:3226-3236(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHAF1A.
    14. "Role of human ribosomal RNA (rRNA) promoter methylation and of methyl-CpG-binding protein MBD2 in the suppression of rRNA gene expression."
      Ghoshal K., Majumder S., Datta J., Motiwala T., Bai S., Sharma S.M., Frankel W., Jacob S.T.
      J. Biol. Chem. 279:6783-6793(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly."
      Sarraf S.A., Stancheva I.
      Mol. Cell 15:595-605(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SETDB1 AND CHAF1A.
    16. "Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins."
      Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.
      J. Biol. Chem. 280:13928-13935(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AFT7IP AND AFT7IP2, MUTAGENESIS OF ILE-576.
    17. "Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins."
      Lyst M.J., Nan X., Stancheva I.
      EMBO J. 25:5317-5328(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETDB1, PHOSPHORYLATION, SUMOYLATION AT LYS-499 AND LYS-538, MUTAGENESIS OF LYS-499; GLU-501; LYS-538 AND GLU-540.
    18. "Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation."
      Uchimura Y., Ichimura T., Uwada J., Tachibana T., Sugahara S., Nakao M., Saitoh H.
      J. Biol. Chem. 281:23180-23190(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, INTERACTION WITH AFT7IP.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: INTERACTION WITH BAHD1.
    21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "Solution structure of the methyl-CpG-binding domain of the methylation-dependent transcriptional repressor MBD1."
      Ohki I., Shimotake N., Fujita N., Nakao M., Shirakawa M.
      EMBO J. 18:6653-6661(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-75 IN COMPLEX WITH METHYLATED DNA, MUTAGENESIS OF ARG-30; ASP-32; TYR-34; ARG-44; SER-45; TYR-52 AND PHE-64.
    24. "Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin."
      Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I., Shirakawa M., Kawasuji M., Nakao M.
      Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-75 IN COMPLEX WITH METHYLATED DNA, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MPG.

    Entry informationi

    Entry nameiMBD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UIS9
    Secondary accession number(s): A4UTZ0
    , B4DXJ5, E9PEC5, K7ELI2, K7EQZ4, K7ESN0, O15248, O95241, Q7Z7B5, Q8N4W4, Q9UNZ6, Q9UNZ7, Q9UNZ8, Q9UNZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3