Q9UIS9 (MBD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MBD1
Synonyms:	CXXC3, PCM1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	605 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 and isoform 2 can also repress transcription from unmethylated promoters. Ref.1 Ref.3 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.24
Subunit structure	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. Ref.1 Ref.4 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.24
Subcellular location	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. Ref.1 Ref.3 Ref.10 Ref.11 Ref.14 Ref.24
Tissue specificity	Widely expressed. Ref.1
Induction	Up-regulated by interferon. Ref.4
Domain	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.
Post-translational modification	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. Ref.17 Ref.18
Sequence similarities	Contains 3 CXXC-type zinc fingers. Contains 1 MBD (methyl-CpG-binding) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of transcription, DNA-dependent Non-traceable author statement Ref.3. Source: UniProtKB transcription from RNA polymerase II promoter Traceable author statement Ref.9. Source: ProtInc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara heterochromatin Inferred from electronic annotation. Source: Compara nuclear matrix Inferred from sequence or structural similarity. Source: UniProtKB nuclear speck Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	methyl-CpG binding Non-traceable author statement Ref.3. Source: UniProtKB sequence-specific DNA binding transcription factor activity Traceable author statement PubMed 10866667. Source: ProtInc transcription corepressor activity Traceable author statement PubMed 10866667. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBX5	P45973	5	EBI-867196,EBI-78219
HDAC1	Q13547	2	EBI-867196,EBI-301834
HDAC2	Q92769	2	EBI-867196,EBI-301821
HDAC3	O15379	3	EBI-867196,EBI-607682
HTT	P42858	2	EBI-867196,EBI-466029
PML-RAR	Q15156	4	EBI-867196,EBI-867256
SUV39H1	O43463	5	EBI-867196,EBI-349968

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UIS9-1)

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.

Isoform 2 (identifier: Q9UIS9-2)

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

Isoform 4 (identifier: Q9UIS9-4)

Also known as: MBD1v3;

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

Isoform 5 (identifier: Q9UIS9-5)

Also known as: PCM1;

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

Isoform 6 (identifier: Q9UIS9-6)

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.

Isoform 7 (identifier: Q9UIS9-7)

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

Isoform 8 (identifier: Q9UIS9-8)

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

Isoform 9 (identifier: Q9UIS9-9)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 605

605

Methyl-CpG-binding domain protein 1

PRO_0000096258

Regions

Domain

1 – 69

69

MBD

Zinc finger

169 – 216

48

CXXC-type 1

Zinc finger

217 – 263

47

CXXC-type 2

Zinc finger

330 – 378

49

CXXC-type 3

Region

529 – 592

64

TRD

Motif

84 – 88

5

Nuclear localization signal Potential

Compositional bias

284 – 313

30

Pro-rich

Amino acid modifications

Modified residue

399

1

Phosphoserine Ref.19 Ref.21

Cross-link

499

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.17

Cross-link

538

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.17

Natural variations

Alternative sequence

173 – 221

49

Missing in isoform 5.

VSP_011064

Alternative sequence

264

1

R → RHLAHRLRRRHQRCQRRTPL AVAPPT in isoform 9.

VSP_042812

Alternative sequence

304 – 326

23

Missing in isoform 2 and isoform 8.

VSP_011065

Alternative sequence

327 – 382

56

Missing in isoform 4 and isoform 7.

VSP_011066

Alternative sequence

483 – 528

46

Missing in isoform 2, isoform 4, isoform 6 and isoform 8.

VSP_011068

Alternative sequence

573 – 596

24

ITEIF…PRSKD → EPTTQPQYSGNFDNDLYEIY LIDI in isoform 6.

VSP_011069

Alternative sequence

593 – 605

13

RSKDL…GARKQ → SLQGRHSGREDGCKVWETED TVEPTSTSWNPRGWPGTHVS LSPPPASMMWVSCRRSWCPS SQS in isoform 2.

VSP_011070

Alternative sequence

597 – 605

9

Missing in isoform 6.

VSP_011071

Natural variant

401

1

P → A. Ref.2
Corresponds to variant rs125555 [ dbSNP | Ensembl ].

VAR_019513

Experimental info

Mutagenesis

22

1

R → A: Abolishes binding to methylated DNA.

Mutagenesis

30

1

R → A: Strongly reduces binding to methylated DNA. Ref.23

Mutagenesis

32

1

D → A: Strongly reduces binding to methylated DNA. Ref.23

Mutagenesis

34

1

Y → A: Reduces binding to methylated DNA. Ref.23

Mutagenesis

44

1

R → A: Abolishes binding to methylated DNA. Ref.23

Mutagenesis

45

1

S → A: Slightly reduces binding to methylated DNA. Ref.23

Mutagenesis

52

1

Y → A: No effect. Ref.23

Mutagenesis

64

1

F → A: Disrupts tertiary structure and abolishes DNA binding. Ref.23

Mutagenesis

499

1

K → A: Abolishes sumoylation; when associated with A-538. Ref.17

Mutagenesis

501

1

E → A: Abolishes sumoylation; when associated with A-540. Ref.17

Mutagenesis

538

1

K → A: Abolishes sumoylation; when associated with A-499. Ref.17

Mutagenesis

540

1

E → A: Abolishes sumoylation; when associated with A-501. Ref.17

Mutagenesis

576

1

I → R: Abolishes interaction with AFT7IP and subsequent transcription repression activity. Ref.16

Sequence conflict

239

1

H → R in ABP02056. Ref.5

Sequence conflict

330

1

T → M in ABP02056. Ref.5

Sequence conflict

348 – 349

2

MD → NG in CAA71735. Ref.1

Sequence conflict

348 – 349

2

MD → NG in AAD51442. Ref.3

Sequence conflict

348 – 349

2

MD → NG in AAD51443. Ref.3

Sequence conflict

489

1

L → M in CAA71735. Ref.1

Isoform 7:

Sequence conflict

327

1

K → Q in AAD51444. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

605

Helix Strand Turn

Details...

Beta strand

5 – 7

3

Turn

9 – 11

3

Beta strand

16 – 19

4

Beta strand

21 – 25

5

Beta strand

33 – 36

4

Beta strand

38 – 40

3

Helix

47 – 53

7

Beta strand

55 – 57

3

Turn

64 – 66

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (MBD1v1) [UniParc]. Last modified July 19, 2004. Version 2. Checksum: 665732782CC6A32A	FASTA	605	66,607
	10 20 30 40 50 60 MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT RYLGPACDLT 70 80 90 100 110 120 LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV GPQSGEVRKE APRDETKADT 130 140 150 160 170 180 DTAPASFPAP GCCENCGISF SGDGTQRQRL KTLCKDCRAQ RIAFNREQRM FKRVGCGECA 190 200 210 220 230 240 ACQVTEDCGA CSTCLLQLPH DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC 250 260 270 280 290 300 PICLRPPRPG LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP 310 320 330 340 350 360 TEPHPRALAP SPPAEFIYYC VDEDELQPYT NRRQNRKCGA CAACLRRMDC GRCDFCCDKP 370 380 390 400 410 420 KFGGSNQKRQ KCRWRQCLQF AMKRLLPSVW SESEDGAGSP PPYRRRKRPS SARRHHLGPT 430 440 450 460 470 480 LKPTLATRTA QPDHTQAPTK QEAGGGFVLP PPGTDLVFLR EGASSPVQVP GPVAASTEAL 490 500 510 520 530 540 LQEAQCSGLS WVVALPQVKQ EKADTQDEWT PGTAVLTSPV LVPGCPSKAV DPGLPSVKQE 550 560 570 580 590 600 PPDPEEDKEE NKDDSASKLA PEEEAGGAGT PVITEIFSLG GTRFRDTAVW LPRSKDLKKP GARKQ
	Isoform 2 (MBD1v2) [UniParc]. Checksum: B77C386F65EA8718	FASTA	586	64,677
	10 20 30 40 50 60 MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT RYLGPACDLT 70 80 90 100 110 120 LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV GPQSGEVRKE APRDETKADT 130 140 150 160 170 180 DTAPASFPAP GCCENCGISF SGDGTQRQRL KTLCKDCRAQ RIAFNREQRM FKRVGCGECA 190 200 210 220 230 240 ACQVTEDCGA CSTCLLQLPH DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC 250 260 270 280 290 300 PICLRPPRPG LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP 310 320 330 340 350 360 TEPQPYTNRR QNRKCGACAA CLRRMDCGRC DFCCDKPKFG GSNQKRQKCR WRQCLQFAMK 370 380 390 400 410 420 RLLPSVWSES EDGAGSPPPY RRRKRPSSAR RHHLGPTLKP TLATRTAQPD HTQAPTKQEA 430 440 450 460 470 480 GGGFVLPPPG TDLVFLREGA SSPVQVPGPV AASTEALLQA VDPGLPSVKQ EPPDPEEDKE 490 500 510 520 530 540 ENKDDSASKL APEEEAGGAG TPVITEIFSL GGTRFRDTAV WLPSLQGRHS GREDGCKVWE 550 560 570 580 TEDTVEPTST SWNPRGWPGT HVSLSPPPAS MMWVSCRRSW CPSSQS
	Isoform 4 (MBD1v3) [UniParc]. Checksum: C5D0267B1D464ACD	FASTA	503	55,167
	10 20 30 40 50 60 MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT RYLGPACDLT 70 80 90 100 110 120 LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV GPQSGEVRKE APRDETKADT 130 140 150 160 170 180 DTAPASFPAP GCCENCGISF SGDGTQRQRL KTLCKDCRAQ RIAFNREQRM FKRVGCGECA 190 200 210 220 230 240 ACQVTEDCGA CSTCLLQLPH DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC 250 260 270 280 290 300 PICLRPPRPG LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP 310 320 330 340 350 360 TEPHPRALAP SPPAEFIYYC VDEDELKRLL PSVWSESEDG AGSPPPYRRR KRPSSARRHH 370 380 390 400 410 420 LGPTLKPTLA TRTAQPDHTQ APTKQEAGGG FVLPPPGTDL VFLREGASSP VQVPGPVAAS 430 440 450 460 470 480 TEALLQAVDP GLPSVKQEPP DPEEDKEENK DDSASKLAPE EEAGGAGTPV ITEIFSLGGT 490 500 RFRDTAVWLP RSKDLKKPGA RKQ
	Isoform 5 (PCM1) [UniParc]. Checksum: 2426F8B3EFD49E3B	FASTA	556	61,265
	10 20 30 40 50 60 MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT RYLGPACDLT 70 80 90 100 110 120 LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV GPQSGEVRKE APRDETKADT 130 140 150 160 170 180 DTAPASFPAP GCCENCGISF SGDGTQRQRL KTLCKDCRAQ RIAFNREQRM FKSRGCGVCR 190 200 210 220 230 240 GCQTQEDCGH CPICLRPPRP GLRRQWKCVQ RRCLRGKHAR RKGGCDSKMA ARRRPGAQPL 250 260 270 280 290 300 PPPPPSQSPE PTEPHPRALA PSPPAEFIYY CVDEDELQPY TNRRQNRKCG ACAACLRRMD 310 320 330 340 350 360 CGRCDFCCDK PKFGGSNQKR QKCRWRQCLQ FAMKRLLPSV WSESEDGAGS PPPYRRRKRP 370 380 390 400 410 420 SSARRHHLGP TLKPTLATRT AQPDHTQAPT KQEAGGGFVL PPPGTDLVFL REGASSPVQV 430 440 450 460 470 480 PGPVAASTEA LLQEAQCSGL SWVVALPQVK QEKADTQDEW TPGTAVLTSP VLVPGCPSKA 490 500 510 520 530 540 VDPGLPSVKQ EPPDPEEDKE ENKDDSASKL APEEEAGGAG TPVITEIFSL GGTRFRDTAV 550 WLPRSKDLKK PGARKQ
	Isoform 6 (MBD1v6) [UniParc]. Checksum: 34194D340ED94FAB	FASTA	550	60,848
	10 20 30 40 50 60 MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT RYLGPACDLT 70 80 90 100 110 120 LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV GPQSGEVRKE APRDETKADT 130 140 150 160 170 180 DTAPASFPAP GCCENCGISF SGDGTQRQRL KTLCKDCRAQ RIAFNREQRM FKRVGCGECA 190 200 210 220 230 240 ACQVTEDCGA CSTCLLQLPH DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC 250 260 270 280 290 300 PICLRPPRPG LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP 310 320 330 340 350 360 TEPHPRALAP SPPAEFIYYC VDEDELQPYT NRRQNRKCGA CAACLRRMDC GRCDFCCDKP 370 380 390 400 410 420 KFGGSNQKRQ KCRWRQCLQF AMKRLLPSVW SESEDGAGSP PPYRRRKRPS SARRHHLGPT 430 440 450 460 470 480 LKPTLATRTA QPDHTQAPTK QEAGGGFVLP PPGTDLVFLR EGASSPVQVP GPVAASTEAL 490 500 510 520 530 540 LQAVDPGLPS VKQEPPDPEE DKEENKDDSA SKLAPEEEAG GAGTPVEPTT QPQYSGNFDN 550 DLYEIYLIDI
	Isoform 7 [UniParc]. Checksum: 45456E4E96182B5C	FASTA	549	60,001
	10 20 30 40 50 60 MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT RYLGPACDLT 70 80 90 100 110 120 LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV GPQSGEVRKE APRDETKADT 130 140 150 160 170 180 DTAPASFPAP GCCENCGISF SGDGTQRQRL KTLCKDCRAQ RIAFNREQRM FKRVGCGECA 190 200 210 220 230 240 ACQVTEDCGA CSTCLLQLPH DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC 250 260 270 280 290 300 PICLRPPRPG LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP 310 320 330 340 350 360 TEPHPRALAP SPPAEFIYYC VDEDELKRLL PSVWSESEDG AGSPPPYRRR KRPSSARRHH 370 380 390 400 410 420 LGPTLKPTLA TRTAQPDHTQ APTKQEAGGG FVLPPPGTDL VFLREGASSP VQVPGPVAAS 430 440 450 460 470 480 TEALLQEAQC SGLSWVVALP QVKQEKADTQ DEWTPGTAVL TSPVLVPGCP SKAVDPGLPS 490 500 510 520 530 540 VKQEPPDPEE DKEENKDDSA SKLAPEEEAG GAGTPVITEI FSLGGTRFRD TAVWLPRSKD LKKPGARKQ
	Isoform 8 [UniParc]. Checksum: 9ED6B5AEF1FF8BD9	FASTA	536	59,158
	10 20 30 40 50 60 MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT RYLGPACDLT 70 80 90 100 110 120 LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV GPQSGEVRKE APRDETKADT 130 140 150 160 170 180 DTAPASFPAP GCCENCGISF SGDGTQRQRL KTLCKDCRAQ RIAFNREQRM FKRVGCGECA 190 200 210 220 230 240 ACQVTEDCGA CSTCLLQLPH DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC 250 260 270 280 290 300 PICLRPPRPG LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP 310 320 330 340 350 360 TEPQPYTNRR QNRKCGACAA CLRRMDCGRC DFCCDKPKFG GSNQKRQKCR WRQCLQFAMK 370 380 390 400 410 420 RLLPSVWSES EDGAGSPPPY RRRKRPSSAR RHHLGPTLKP TLATRTAQPD HTQAPTKQEA 430 440 450 460 470 480 GGGFVLPPPG TDLVFLREGA SSPVQVPGPV AASTEALLQA VDPGLPSVKQ EPPDPEEDKE 490 500 510 520 530 ENKDDSASKL APEEEAGGAG TPVITEIFSL GGTRFRDTAV WLPRSKDLKK PGARKQ
	Isoform 9 [UniParc]. Checksum: 23AF6E138EA8AD82	FASTA	630	69,617
	10 20 30 40 50 60 MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT RYLGPACDLT 70 80 90 100 110 120 LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV GPQSGEVRKE APRDETKADT 130 140 150 160 170 180 DTAPASFPAP GCCENCGISF SGDGTQRQRL KTLCKDCRAQ RIAFNREQRM FKRVGCGECA 190 200 210 220 230 240 ACQVTEDCGA CSTCLLQLPH DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC 250 260 270 280 290 300 PICLRPPRPG LRRQWKCVQR RCLRHLAHRL RRRHQRCQRR TPLAVAPPTG KHARRKGGCD 310 320 330 340 350 360 SKMAARRRPG AQPLPPPPPS QSPEPTEPHP RALAPSPPAE FIYYCVDEDE LQPYTNRRQN 370 380 390 400 410 420 RKCGACAACL RRMDCGRCDF CCDKPKFGGS NQKRQKCRWR QCLQFAMKRL LPSVWSESED 430 440 450 460 470 480 GAGSPPPYRR RKRPSSARRH HLGPTLKPTL ATRTAQPDHT QAPTKQEAGG GFVLPPPGTD 490 500 510 520 530 540 LVFLREGASS PVQVPGPVAA STEALLQEAQ CSGLSWVVAL PQVKQEKADT QDEWTPGTAV 550 560 570 580 590 600 LTSPVLVPGC PSKAVDPGLP SVKQEPPDPE EDKEENKDDS ASKLAPEEEA GGAGTPVITE 610 620 630 IFSLGGTRFR DTAVWLPRSK DLKKPGARKQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] 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]	"MCAF mediates MBD1-dependent transcriptional repression." Fujita N., Watanabe S., Ichimura T., Ohkuma Y., Chiba T., Saya H., Nakao M. Mol. Cell. Biol. 23:2834-2843(2003) [PubMed] [Europe PMC] [Abstract] 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Human BAHD1 promotes heterochromatic gene silencing." Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M., Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J., Cossart P. Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00438701.
IPI00438702.
IPI00438703.
IPI00438705.
IPI00438706.
IPI00438707.
IPI00854577.
IPI00941642.

RefSeq

NP_001191065.1. NM_001204136.1.
NP_001191066.1. NM_001204137.1.
NP_001191067.1. NM_001204138.1.
NP_001191068.1. NM_001204139.1.
NP_001191069.1. NM_001204140.1.
NP_001191070.1. NM_001204141.1.
NP_001191071.1. NM_001204142.1.
NP_001191072.1. NM_001204143.1.
NP_001191080.1. NM_001204151.1.
NP_002375.1. NM_002384.2.
NP_056669.2. NM_015844.2.
NP_056670.2. NM_015845.3.
NP_056671.2. NM_015846.3.
NP_056723.2. NM_015847.3.

UniGene

Hs.405610.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D9N	NMR	-	A	1-75	[»]
1IG4	NMR	-	A	1-75	[»]

ProteinModelPortal

Q9UIS9.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UIS9. 9 interactions.

MINT

MINT-2860643.

PTM databases

PhosphoSite

Q9UIS9.

Polymorphism databases

DMDM

50401200.

Proteomic databases

PaxDb

Q9UIS9.

PRIDE

Q9UIS9.

Protocols and materials databases

DNASU

4152.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000269468; ENSP00000269468; ENSG00000141644.
ENST00000269471; ENSP00000269471; ENSG00000141644.
ENST00000339998; ENSP00000339546; ENSG00000141644.
ENST00000347968; ENSP00000285102; ENSG00000141644.
ENST00000349085; ENSP00000342531; ENSG00000141644.
ENST00000353909; ENSP00000269469; ENSG00000141644.
ENST00000382948; ENSP00000372407; ENSG00000141644.
ENST00000398488; ENSP00000381502; ENSG00000141644.
ENST00000398493; ENSP00000381506; ENSG00000141644.
ENST00000436910; ENSP00000409561; ENSG00000141644.
ENST00000457839; ENSP00000405268; ENSG00000141644.
ENST00000585595; ENSP00000468430; ENSG00000141644.
ENST00000588937; ENSP00000467763; ENSG00000141644.
ENST00000591416; ENSP00000467017; ENSG00000141644.
ENST00000591535; ENSP00000465923; ENSG00000141644.

GeneID

4152.

KEGG

hsa:4152.

UCSC

uc002leg.3. human.
uc002leh.4. human.
uc002lei.4. human.
uc002lej.4. human.
uc002lel.4. human.
uc002len.3. human.
uc010dox.1. human.

Organism-specific databases

CTD

4152.

GeneCards

GC18M047795.

HGNC

HGNC:6916. MBD1.

HPA

CAB009017.
CAB036003.

MIM

156535. gene.

neXtProt

NX_Q9UIS9.

PharmGKB

PA30659.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG145219.

HOVERGEN

HBG052416.

InParanoid

Q9UIS9.

KO

K11589.

PhylomeDB

Q9UIS9.

Gene expression databases

ArrayExpress

Q9UIS9.

Bgee

Q9UIS9.

CleanEx

HS_PCM1.

Genevestigator

Q9UIS9.

GermOnline

ENSG00000141644. Homo sapiens.

Family and domain databases

Gene3D

3.30.890.10. 1 hit.

InterPro

IPR016177. DNA-bd_integrase-typ.
IPR001739. Methyl_CpG_DNA-bd.
IPR002857. Znf_CXXC.
[Graphical view]

Pfam

PF01429. MBD. 1 hit.
PF02008. zf-CXXC. 3 hits.
[Graphical view]

SMART

SM00391. MBD. 1 hit.
[Graphical view]

SUPFAM

SSF54171. DNA-binding_integrase-type. 1 hit.

PROSITE

PS50982. MBD. 1 hit.
PS51058. ZF_CXXC. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9UIS9.

GenomeRNAi

4152.

NextBio

16330.

SOURCE

Search...

Entry information

Entry name

MBD1_HUMAN

Accession

Primary (citable) accession number: Q9UIS9
Secondary accession number(s): A4UTZ0 , B4DXJ5, E9PEC5, O15248, O95241, Q7Z7B5, Q8N4W4, Q9UNZ6, Q9UNZ7, Q9UNZ8, Q9UNZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.