Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methyl-CpG-binding domain protein 4

Gene

MBD4

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

Functioni

Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei560 – 5601By similarity

GO - Molecular functioni

  • endodeoxyribonuclease activity Source: ProtInc
  • pyrimidine-specific mismatch base pair DNA N-glycosylase activity Source: MGI
  • satellite DNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-110328. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
R-HSA-110329. Cleavage of the damaged pyrimidine.
R-HSA-110357. Displacement of DNA glycosylase by APEX1.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-CpG-binding domain protein 4 (EC:3.2.2.-)
Alternative name(s):
Methyl-CpG-binding endonuclease 1
Methyl-CpG-binding protein MBD4
Mismatch-specific DNA N-glycosylase
Gene namesi
Name:MBD4
Synonyms:MED1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6919. MBD4.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: GO_Central
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580Methyl-CpG-binding domain protein 4PRO_0000096264Add
BLAST

Proteomic databases

EPDiO95243.
MaxQBiO95243.
PaxDbiO95243.
PRIDEiO95243.
TopDownProteomicsiO95243-3. [O95243-3]

PTM databases

iPTMnetiO95243.
PhosphoSiteiO95243.

Expressioni

Gene expression databases

BgeeiO95243.
CleanExiHS_MBD4.
HS_MED1.
ExpressionAtlasiO95243. baseline and differential.
GenevisibleiO95243. HS.

Organism-specific databases

HPAiHPA002031.

Interactioni

Subunit structurei

Interacts with MLH1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FADDQ131586EBI-348011,EBI-494804

Protein-protein interaction databases

BioGridi114444. 25 interactions.
IntActiO95243. 14 interactions.
MINTiMINT-264766.
STRINGi9606.ENSP00000249910.

Structurei

Secondary structure

1
580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi91 – 966Combined sources
Turni101 – 1044Combined sources
Beta strandi106 – 1116Combined sources
Helixi121 – 13010Combined sources
Helixi138 – 1403Combined sources
Helixi449 – 4524Combined sources
Helixi456 – 46510Combined sources
Turni466 – 4683Combined sources
Helixi471 – 48414Combined sources
Helixi488 – 4914Combined sources
Helixi496 – 5038Combined sources
Helixi504 – 5063Combined sources
Helixi509 – 52517Combined sources
Helixi531 – 5333Combined sources
Helixi539 – 54810Combined sources
Helixi553 – 5553Combined sources
Helixi561 – 57717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MOENMR-A80-148[»]
3IHOX-ray2.70A437-574[»]
4DK9X-ray2.76A426-580[»]
4E9EX-ray1.90A427-580[»]
4E9FX-ray1.79A427-580[»]
4E9GX-ray2.35A427-580[»]
4E9HX-ray3.00A427-580[»]
4EA4X-ray2.00A427-574[»]
4EA5X-ray2.14A427-580[»]
4LG7X-ray2.50A83-149[»]
4OFAX-ray1.55A426-580[»]
4OFEX-ray2.15A426-580[»]
4OFHX-ray2.22A426-580[»]
ProteinModelPortaliO95243.
SMRiO95243. Positions 83-145, 437-574.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95243.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 14873MBDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4161. Eukaryota.
ENOG4111HPQ. LUCA.
GeneTreeiENSGT00530000063687.
HOGENOMiHOG000113489.
HOVERGENiHBG052418.
InParanoidiO95243.
KOiK10801.
OMAiTADWRDV.
OrthoDBiEOG74N5J9.
PhylomeDBiO95243.
TreeFamiTF329176.

Family and domain databases

Gene3Di1.10.340.30. 1 hit.
3.30.890.10. 1 hit.
InterProiIPR016177. DNA-bd_dom.
IPR011257. DNA_glycosylase.
IPR017352. MBD4.
IPR001739. Methyl_CpG_DNA-bd.
[Graphical view]
PfamiPF01429. MBD. 1 hit.
[Graphical view]
PIRSFiPIRSF038005. Methyl_CpG_bd_MBD4. 1 hit.
SMARTiSM00391. MBD. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
SSF54171. SSF54171. 1 hit.
PROSITEiPS50982. MBD. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95243-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MGTTGLESLS LGDRGAAPTV TSSERLVPDP PNDLRKEDVA MELERVGEDE
60 70 80 90 100
EQMMIKRSSE CNPLLQEPIA SAQFGATAGT ECRKSVPCGW ERVVKQRLFG
110 120 130 140 150
KTAGRFDVYF ISPQGLKFRS KSSLANYLHK NGETSLKPED FDFTVLSKRG
160 170 180 190 200
IKSRYKDCSM AALTSHLQNQ SNNSNWNLRT RSKCKKDVFM PPSSSSELQE
210 220 230 240 250
SRGLSNFTST HLLLKEDEGV DDVNFRKVRK PKGKVTILKG IPIKKTKKGC
260 270 280 290 300
RKSCSGFVQS DSKRESVCNK ADAESEPVAQ KSQLDRTVCI SDAGACGETL
310 320 330 340 350
SVTSEENSLV KKKERSLSSG SNFCSEQKTS GIINKFCSAK DSEHNEKYED
360 370 380 390 400
TFLESEEIGT KVEVVERKEH LHTDILKRGS EMDNNCSPTR KDFTGEKIFQ
410 420 430 440 450
EDTIPRTQIE RRKTSLYFSS KYNKEALSPP RRKAFKKWTP PRSPFNLVQE
460 470 480 490 500
TLFHDPWKLL IATIFLNRTS GKMAIPVLWK FLEKYPSAEV ARTADWRDVS
510 520 530 540 550
ELLKPLGLYD LRAKTIVKFS DEYLTKQWKY PIELHGIGKY GNDSYRIFCV
560 570 580
NEWKQVHPED HKLNKYHDWL WENHEKLSLS
Length:580
Mass (Da):66,051
Last modified:May 1, 1999 - v1
Checksum:iBF16FB21A34B8E5F
GO
Isoform 2 (identifier: O95243-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     395-400: Missing.

Show »
Length:574
Mass (Da):65,348
Checksum:i33809A26A2E61A26
GO
Isoform 3 (identifier: O95243-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     539-540: KY → AP
     541-580: Missing.

Note: No experimental confirmation available.
Show »
Length:540
Mass (Da):60,949
Checksum:i3131CE4F9A488371
GO
Isoform 5 (identifier: O95243-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     557-580: HPEDHKLNKYHDWLWENHEKLSLS → RLTPIHNSAHLVSEAK

Note: No experimental confirmation available.
Show »
Length:572
Mass (Da):64,768
Checksum:i8550E8B5D9372097
GO
Isoform 4 (identifier: O95243-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     83-401: RKSVPCGWER...DFTGEKIFQE → Q

Note: Possesses uracil DNA glycosylase but not thymine DNA glycosylase activity.
Show »
Length:262
Mass (Da):30,316
Checksum:i578F5642D59D353D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511E → G in BAG64144 (PubMed:14702039).Curated
Sequence conflicti359 – 3591G → R in BAG64144 (PubMed:14702039).Curated
Sequence conflicti387 – 3871S → L in BAG64144 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611C → R.
Corresponds to variant rs2307296 [ dbSNP | Ensembl ].
VAR_029306
Natural varianti273 – 2731A → S.1 Publication
Corresponds to variant rs10342 [ dbSNP | Ensembl ].
VAR_019357
Natural varianti273 – 2731A → T.
Corresponds to variant rs10342 [ dbSNP | Ensembl ].
VAR_019514
Natural varianti342 – 3421S → P.1 Publication
Corresponds to variant rs2307289 [ dbSNP | Ensembl ].
VAR_019358
Natural varianti346 – 3461E → K.1 Publication
Corresponds to variant rs140693 [ dbSNP | Ensembl ].
VAR_019359
Natural varianti358 – 3581I → T.
Corresponds to variant rs2307298 [ dbSNP | Ensembl ].
VAR_019515
Natural varianti568 – 5681D → H.1 Publication
Corresponds to variant rs2307293 [ dbSNP | Ensembl ].
VAR_019360

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei83 – 401319RKSVP…KIFQE → Q in isoform 4. 1 PublicationVSP_054845Add
BLAST
Alternative sequencei395 – 4006Missing in isoform 2. 2 PublicationsVSP_010816
Alternative sequencei539 – 5402KY → AP in isoform 3. 1 PublicationVSP_010817
Alternative sequencei541 – 58040Missing in isoform 3. 1 PublicationVSP_010818Add
BLAST
Alternative sequencei557 – 58024HPEDH…KLSLS → RLTPIHNSAHLVSEAK in isoform 5. 1 PublicationVSP_054846Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072250 mRNA. Translation: AAC68879.1.
AF120999, AF120997, AF120998 Genomic DNA. Translation: AAD50374.1.
AF114784 mRNA. Translation: AAD22195.1.
AM180876 mRNA. Translation: CAJ55826.1.
AF532602 mRNA. Translation: AAP97338.1.
AK303013 mRNA. Translation: BAG64144.1.
CR450305 mRNA. Translation: CAG29301.1.
AF494057 Genomic DNA. Translation: AAM00008.1.
AL449212 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79251.1.
CH471052 Genomic DNA. Translation: EAW79253.1.
CH471052 Genomic DNA. Translation: EAW79254.1.
CH471052 Genomic DNA. Translation: EAW79255.1.
BC011752 mRNA. Translation: AAH11752.1.
CCDSiCCDS3058.1. [O95243-1]
CCDS63766.1. [O95243-5]
CCDS63767.1. [O95243-3]
CCDS63768.1. [O95243-2]
CCDS63769.1. [O95243-6]
RefSeqiNP_001263199.1. NM_001276270.1. [O95243-2]
NP_001263200.1. NM_001276271.1. [O95243-5]
NP_001263201.1. NM_001276272.1. [O95243-3]
NP_001263202.1. NM_001276273.1. [O95243-6]
NP_003916.1. NM_003925.2. [O95243-1]
UniGeneiHs.35947.

Genome annotation databases

EnsembliENST00000249910; ENSP00000249910; ENSG00000129071. [O95243-1]
ENST00000393278; ENSP00000376959; ENSG00000129071. [O95243-6]
ENST00000429544; ENSP00000394080; ENSG00000129071. [O95243-2]
ENST00000503197; ENSP00000424873; ENSG00000129071. [O95243-3]
ENST00000507208; ENSP00000422327; ENSG00000129071. [O95243-5]
GeneIDi8930.
KEGGihsa:8930.
UCSCiuc003emh.3. human. [O95243-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072250 mRNA. Translation: AAC68879.1.
AF120999, AF120997, AF120998 Genomic DNA. Translation: AAD50374.1.
AF114784 mRNA. Translation: AAD22195.1.
AM180876 mRNA. Translation: CAJ55826.1.
AF532602 mRNA. Translation: AAP97338.1.
AK303013 mRNA. Translation: BAG64144.1.
CR450305 mRNA. Translation: CAG29301.1.
AF494057 Genomic DNA. Translation: AAM00008.1.
AL449212 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79251.1.
CH471052 Genomic DNA. Translation: EAW79253.1.
CH471052 Genomic DNA. Translation: EAW79254.1.
CH471052 Genomic DNA. Translation: EAW79255.1.
BC011752 mRNA. Translation: AAH11752.1.
CCDSiCCDS3058.1. [O95243-1]
CCDS63766.1. [O95243-5]
CCDS63767.1. [O95243-3]
CCDS63768.1. [O95243-2]
CCDS63769.1. [O95243-6]
RefSeqiNP_001263199.1. NM_001276270.1. [O95243-2]
NP_001263200.1. NM_001276271.1. [O95243-5]
NP_001263201.1. NM_001276272.1. [O95243-3]
NP_001263202.1. NM_001276273.1. [O95243-6]
NP_003916.1. NM_003925.2. [O95243-1]
UniGeneiHs.35947.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MOENMR-A80-148[»]
3IHOX-ray2.70A437-574[»]
4DK9X-ray2.76A426-580[»]
4E9EX-ray1.90A427-580[»]
4E9FX-ray1.79A427-580[»]
4E9GX-ray2.35A427-580[»]
4E9HX-ray3.00A427-580[»]
4EA4X-ray2.00A427-574[»]
4EA5X-ray2.14A427-580[»]
4LG7X-ray2.50A83-149[»]
4OFAX-ray1.55A426-580[»]
4OFEX-ray2.15A426-580[»]
4OFHX-ray2.22A426-580[»]
ProteinModelPortaliO95243.
SMRiO95243. Positions 83-145, 437-574.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114444. 25 interactions.
IntActiO95243. 14 interactions.
MINTiMINT-264766.
STRINGi9606.ENSP00000249910.

PTM databases

iPTMnetiO95243.
PhosphoSiteiO95243.

Proteomic databases

EPDiO95243.
MaxQBiO95243.
PaxDbiO95243.
PRIDEiO95243.
TopDownProteomicsiO95243-3. [O95243-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249910; ENSP00000249910; ENSG00000129071. [O95243-1]
ENST00000393278; ENSP00000376959; ENSG00000129071. [O95243-6]
ENST00000429544; ENSP00000394080; ENSG00000129071. [O95243-2]
ENST00000503197; ENSP00000424873; ENSG00000129071. [O95243-3]
ENST00000507208; ENSP00000422327; ENSG00000129071. [O95243-5]
GeneIDi8930.
KEGGihsa:8930.
UCSCiuc003emh.3. human. [O95243-1]

Organism-specific databases

CTDi8930.
GeneCardsiMBD4.
HGNCiHGNC:6919. MBD4.
HPAiHPA002031.
MIMi603574. gene.
neXtProtiNX_O95243.
PharmGKBiPA30663.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4161. Eukaryota.
ENOG4111HPQ. LUCA.
GeneTreeiENSGT00530000063687.
HOGENOMiHOG000113489.
HOVERGENiHBG052418.
InParanoidiO95243.
KOiK10801.
OMAiTADWRDV.
OrthoDBiEOG74N5J9.
PhylomeDBiO95243.
TreeFamiTF329176.

Enzyme and pathway databases

ReactomeiR-HSA-110328. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
R-HSA-110329. Cleavage of the damaged pyrimidine.
R-HSA-110357. Displacement of DNA glycosylase by APEX1.

Miscellaneous databases

EvolutionaryTraceiO95243.
GeneWikiiMBD4.
GenomeRNAii8930.
NextBioi33578.
PROiO95243.
SOURCEiSearch...

Gene expression databases

BgeeiO95243.
CleanExiHS_MBD4.
HS_MED1.
ExpressionAtlasiO95243. baseline and differential.
GenevisibleiO95243. HS.

Family and domain databases

Gene3Di1.10.340.30. 1 hit.
3.30.890.10. 1 hit.
InterProiIPR016177. DNA-bd_dom.
IPR011257. DNA_glycosylase.
IPR017352. MBD4.
IPR001739. Methyl_CpG_DNA-bd.
[Graphical view]
PfamiPF01429. MBD. 1 hit.
[Graphical view]
PIRSFiPIRSF038005. Methyl_CpG_bd_MBD4. 1 hit.
SMARTiSM00391. MBD. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
SSF54171. SSF54171. 1 hit.
PROSITEiPS50982. MBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1).
  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].
  3. "MED1, a novel human methyl-CpG-binding endonuclease, interacts with DNA mismatch repair protein MLH1."
    Bellacosa A., Cicchillitti L., Schepis F., Riccio A., Yeung A.T., Matsumoto Y., Golemis E.A., Genuardi M., Neri G.
    Proc. Natl. Acad. Sci. U.S.A. 96:3969-3974(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MLH1.
    Tissue: Fetal brain.
  4. "The identification of a novel alternatively spliced form of the MBD4 DNA glycosylase."
    Owen R.M., Baker R.D., Bader S., Dunlop M.G., Nicholl I.D.
    Oncol. Rep. 17:111-116(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING.
  5. Guo J.H., Chen L., Yu L.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Lung.
  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 5).
    Tissue: Testis.
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  8. NIEHS SNPs program
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-273; PRO-342; LYS-346 AND HIS-568.
  9. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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 2).
    Tissue: Lung.
  12. "Biphasic kinetics of the human DNA repair protein MED1 (MBD4), a mismatch-specific DNA N-glycosylase."
    Petronzelli F., Riccio A., Markham G.D., Seeholzer S.H., Stoerker J., Genuardi M., Yeung A.T., Matsumoto Y., Bellacosa A.
    J. Biol. Chem. 275:32422-32429(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosis."
    Screaton R.A., Kiessling S., Sansom O.J., Millar C.B., Maddison K., Bird A., Clarke A.R., Frisch S.M.
    Proc. Natl. Acad. Sci. U.S.A. 100:5211-5216(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FADD.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiMBD4_HUMAN
AccessioniPrimary (citable) accession number: O95243
Secondary accession number(s): B4DZN2
, D3DNC3, D3DNC4, E9PEE4, Q2MD36, Q7Z4T3, Q96F09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 1999
Last modified: April 13, 2016
This is version 135 of the entry and version 1 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 3
    Human chromosome 3: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.