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Q9UIS9

- MBD1_HUMAN

UniProt

Q9UIS9 - MBD1_HUMAN

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Protein

Methyl-CpG-binding domain protein 1

Gene
MBD1, CXXC3, PCM1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1Add
BLAST
Zinc fingeri217 – 26347CXXC-type 2Add
BLAST
Zinc fingeri330 – 37849CXXC-type 3Add
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
Complete GO annotation...

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.6 Publications

GO - Cellular componenti

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

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 – 3991Phosphoserine2 Publications
Cross-linki499 – 499Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki538 – 538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

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 SETDB1.11 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.

Miscellaneous databases

EvolutionaryTraceiQ9UIS9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6969MBDAdd
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi84 – 885Nuclear localization signal Reviewed prediction

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

Zinc finger

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

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. VSP_011064Add
BLAST
Alternative sequencei264 – 2641R → RHLAHRLRRRHQRCQRRTPL AVAPPT in isoform 9. VSP_042812
Alternative sequencei304 – 32623Missing in isoform 2 and isoform 8. VSP_011065Add
BLAST
Alternative sequencei326 – 38257LQPYT…LQFAM → L in isoform 11. VSP_054736Add
BLAST
Alternative sequencei327 – 38256Missing in isoform 4 and isoform 7. VSP_011066Add
BLAST
Alternative sequencei327 – 3271Missing in isoform 10. VSP_054737
Alternative sequencei483 – 52846Missing in isoform 2, isoform 4, isoform 6, isoform 8 and isoform 11. VSP_011068Add
BLAST
Alternative sequencei573 – 59624ITEIF…PRSKD → EPTTQPQYSGNFDNDLYEIY LIDI in isoform 6. VSP_011069Add
BLAST
Alternative sequencei593 – 60513RSKDL…GARKQ → SLQGRHSGREDGCKVWETED TVEPTSTSWNPRGWPGTHVS LSPPPASMMWVSCRRSWCPS SQS in isoform 2 and isoform 12. VSP_011070Add
BLAST
Alternative sequencei594 – 60512SKDLK…GARKQ → YYHLALDWKCNCGYHLCCRS VLVP in isoform 10. VSP_054738Add
BLAST
Alternative sequencei594 – 60512SKDLK…GARKQ → AGTREGKMDVKCGRPRTQWS PRARAGTHEDGLEPMSVSHH LQLR in isoform 11. VSP_054739Add
BLAST
Alternative sequencei597 – 6059Missing in isoform 6. VSP_011071

Sequence conflict

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

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]
ENST00000349085; ENSP00000342531; ENSG00000141644. [Q9UIS9-4]
ENST00000353909; ENSP00000269469; ENSG00000141644. [Q9UIS9-5]
ENST00000382948; ENSP00000372407; ENSG00000141644. [Q9UIS9-1]
ENST00000398488; ENSP00000381502; ENSG00000141644. [Q9UIS9-4]
ENST00000398493; ENSP00000381506; ENSG00000141644. [Q9UIS9-7]
ENST00000436910; ENSP00000409561; ENSG00000141644. [Q9UIS9-8]
ENST00000457839; ENSP00000405268; ENSG00000141644. [Q9UIS9-9]
ENST00000585595; ENSP00000468430; ENSG00000141644. [Q9UIS9-9]
ENST00000585672; ENSP00000466092; ENSG00000141644.
ENST00000587605; ENSP00000468042; ENSG00000141644.
ENST00000588937; ENSP00000467763; ENSG00000141644. [Q9UIS9-2]
ENST00000590208; ENSP00000468785; ENSG00000141644.
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 ]
ENST00000349085 ; ENSP00000342531 ; ENSG00000141644 . [Q9UIS9-4 ]
ENST00000353909 ; ENSP00000269469 ; ENSG00000141644 . [Q9UIS9-5 ]
ENST00000382948 ; ENSP00000372407 ; ENSG00000141644 . [Q9UIS9-1 ]
ENST00000398488 ; ENSP00000381502 ; ENSG00000141644 . [Q9UIS9-4 ]
ENST00000398493 ; ENSP00000381506 ; ENSG00000141644 . [Q9UIS9-7 ]
ENST00000436910 ; ENSP00000409561 ; ENSG00000141644 . [Q9UIS9-8 ]
ENST00000457839 ; ENSP00000405268 ; ENSG00000141644 . [Q9UIS9-9 ]
ENST00000585595 ; ENSP00000468430 ; ENSG00000141644 . [Q9UIS9-9 ]
ENST00000585672 ; ENSP00000466092 ; ENSG00000141644 .
ENST00000587605 ; ENSP00000468042 ; ENSG00000141644 .
ENST00000588937 ; ENSP00000467763 ; ENSG00000141644 . [Q9UIS9-2 ]
ENST00000590208 ; ENSP00000468785 ; ENSG00000141644 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 137 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

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