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

Lethal(3)malignant brain tumor-like protein 1

Gene

L3MBTL1

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

Functioni

Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei355 – 3551Mediates recognition of monomethylated and dimethylated peptides
Sitei358 – 3581Positioned at the entrance of MBT 2 and is required for recognition of monomethylated and dimethylated peptides

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri552 – 57827C2HC-typeAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB
  • nucleosomal histone binding Source: UniProtKB
  • nucleosome binding Source: UniProtKB
  • SAM domain binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

  • chromatin modification Source: UniProtKB
  • hemopoiesis Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of cell cycle Source: UniProtKB
  • regulation of megakaryocyte differentiation Source: UniProtKB
  • regulation of mitotic nuclear division Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Lethal(3)malignant brain tumor-like protein 1
Short name:
H-l(3)mbt
Short name:
H-l(3)mbt protein
Short name:
L(3)mbt-like
Alternative name(s):
L(3)mbt protein homolog
L3MBTL1
Gene namesi
Name:L3MBTL1
Synonyms:KIAA0681, L3MBT, L3MBTL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15905. L3MBTL1.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Excluded from the nucleolus. Does not colocalizes with the PcG protein BMI1, suggesting that these two proteins do not belong to the same complex.

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • condensed chromosome Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi248 – 2481D → N: Does not affect binding to monomethylated and dimethylated peptides. 1 Publication
Mutagenesisi272 – 2721F → A: Does not affect binding to monomethylated and dimethylated peptides. 1 Publication
Mutagenesisi355 – 3551D → A: Abolishes binding to monomethylated and dimethylated peptides. 4 Publications
Mutagenesisi355 – 3551D → N: Strongly impairs binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. 4 Publications
Mutagenesisi358 – 3581N → A: Abolishes binding to monomethylated and dimethylated peptides. 2 Publications
Mutagenesisi358 – 3581N → Q: Strongly impairs binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. 2 Publications
Mutagenesisi363 – 3631C → F or R: Strongly impairs binding to monomethylated and dimethylated peptides. 1 Publication
Mutagenesisi379 – 3791F → A: Abolishes binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. 2 Publications
Mutagenesisi382 – 3821W → L: Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. 1 Publication
Mutagenesisi386 – 3861Y → L: Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. 1 Publication
Mutagenesisi459 – 4591D → N: Does not affect binding to monomethylated and dimethylated peptides. 1 Publication
Mutagenesisi483 – 4831F → A: Does not affect binding to monomethylated and dimethylated peptides. 1 Publication

Organism-specific databases

PharmGKBiPA30260.

Chemistry

ChEMBLiCHEMBL1287622.

Polymorphism and mutation databases

BioMutaiL3MBTL1.
DMDMi325511398.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 752752Lethal(3)malignant brain tumor-like protein 1PRO_0000084452Add
BLAST

Post-translational modificationi

Ubiquitinated in a VCP/p97-dependent way following DNA damage, leading to its removal from DNA damage sites, promoting accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited to DNA damage sites.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ9Y468.
PaxDbiQ9Y468.
PRIDEiQ9Y468.

PTM databases

PhosphoSiteiQ9Y468.

Expressioni

Tissue specificityi

Widely expressed. Expression is reduced in colorectal cancer cell line SW480 and promyelocytic leukemia cell line HL-60.1 Publication

Developmental stagei

In interphase cells, it is scattered throughout the nucleoplasm. In mitotic cells, it strongly associates with condensed chromosomes from the prophase to telophase.

Gene expression databases

BgeeiQ9Y468.
CleanExiHS_L3MBTL.
ExpressionAtlasiQ9Y468. baseline and differential.
GenevisibleiQ9Y468. HS.

Interactioni

Subunit structurei

Homodimer. Interacts with RB1/RB (when monomethylated at 'Lys-860'). Interacts with p53/TP53 (when monomethylated at 'Lys-382'). Interacts with CBX3, ETV6, KMT5A and VCP/p97.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST1H1EP104127EBI-1265089,EBI-358163
HIST1H3FP684312EBI-1265089,EBI-79722
HIST1H4KP628054EBI-1265089,EBI-302023

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB
  • nucleosomal histone binding Source: UniProtKB
  • nucleosome binding Source: UniProtKB
  • SAM domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117486. 43 interactions.
DIPiDIP-29628N.
IntActiQ9Y468. 5 interactions.
MINTiMINT-2830196.
STRINGi9606.ENSP00000398516.

Chemistry

BindingDBiQ9Y468.

Structurei

Secondary structure

1
752
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi208 – 2158Combined sources
Helixi222 – 2243Combined sources
Helixi227 – 2304Combined sources
Beta strandi243 – 2486Combined sources
Beta strandi251 – 26414Combined sources
Beta strandi267 – 2726Combined sources
Helixi277 – 2793Combined sources
Beta strandi281 – 2844Combined sources
Beta strandi288 – 2914Combined sources
Helixi295 – 2995Combined sources
Helixi311 – 3133Combined sources
Helixi316 – 3238Combined sources
Helixi330 – 3323Combined sources
Beta strandi350 – 3545Combined sources
Turni356 – 3594Combined sources
Beta strandi362 – 37110Combined sources
Beta strandi374 – 3796Combined sources
Helixi384 – 3863Combined sources
Beta strandi388 – 3903Combined sources
Helixi402 – 4065Combined sources
Helixi419 – 4213Combined sources
Helixi424 – 4318Combined sources
Helixi438 – 4403Combined sources
Beta strandi454 – 4585Combined sources
Beta strandi460 – 4623Combined sources
Beta strandi466 – 4749Combined sources
Beta strandi476 – 4838Combined sources
Helixi488 – 4903Combined sources
Beta strandi492 – 4954Combined sources
Helixi506 – 5105Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OYXX-ray1.85A/B/C197-527[»]
1OZ2X-ray1.55A197-527[»]
1OZ3X-ray1.85A/B/C197-527[»]
2PQWX-ray2.00A200-522[»]
2RHIX-ray1.66A197-526[»]
2RHUX-ray1.90A206-519[»]
2RHXX-ray2.10A197-526[»]
2RHYX-ray1.90A206-519[»]
2RHZX-ray2.20A206-519[»]
2RI2X-ray2.20A206-519[»]
2RI3X-ray2.00A206-519[»]
2RI5X-ray2.00A206-519[»]
2RJCX-ray2.00A/B/C200-530[»]
2RJDX-ray1.65A200-530[»]
2RJEX-ray1.86A/B/C200-530[»]
2RJFX-ray2.05A/C/E200-530[»]
3OQ5X-ray2.50A/B/C191-530[»]
3P8HX-ray2.55A/B/C200-522[»]
3UWNX-ray2.15A200-530[»]
ProteinModelPortaliQ9Y468.
SMRiQ9Y468. Positions 204-581, 683-737.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y468.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati206 – 306101MBT 1Add
BLAST
Repeati314 – 413100MBT 2Add
BLAST
Repeati422 – 51796MBT 3Add
BLAST
Domaini683 – 74765SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni379 – 3868Interaction with monomethylated and dimethylated peptides

Domaini

The MBT repeat 2 specifically recognizes and binds monomethylated and dimethylated proteins. In contrast, it does not bind trimethylated proteins. The MBT repeat 1 does not bind methylated peptides but inserts a proline ring in a Pro-Ser-Ser/Thr sequence context.1 Publication

Sequence similaritiesi

Contains 1 C2HC-type zinc finger.Curated
Contains 3 MBT repeats.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri552 – 57827C2HC-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG3766. Eukaryota.
ENOG410Y4AQ. LUCA.
GeneTreeiENSGT00760000119024.
HOVERGENiHBG071375.
InParanoidiQ9Y468.
OMAiQEDFQTI.
OrthoDBiEOG7FR7FT.
PhylomeDBiQ9Y468.
TreeFamiTF316498.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR002515. Znf_C2HC.
[Graphical view]
PfamiPF02820. MBT. 3 hits.
PF00536. SAM_1. 1 hit.
PF01530. zf-C2HC. 1 hit.
[Graphical view]
SMARTiSM00561. MBT. 3 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS51079. MBT. 3 hits.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

Isoform 4 (identifier: Q9Y468-4) [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
MRRREGHGTD SEMGQGPVRE SQSSDPPALQ FRISEYKPLN MAGVEQPPSP
60 70 80 90 100
ELRQEGVTEY EDGGAPAGDG EAGPQQAEDH PQNPPEDPNQ DPPEDDSTCQ
110 120 130 140 150
CQACGPHQAA GPDLGSSNDG CPQLFQERSV IVENSSGSTS ASELLKPMKK
160 170 180 190 200
RKRREYQSPS EEESEPEAME KQEEGKDPEG QPTASTPESE EWSSSQPATG
210 220 230 240 250
EKKECWSWES YLEEQKAITA PVSLFQDSQA VTHNKNGFKL GMKLEGIDPQ
260 270 280 290 300
HPSMYFILTV AEVCGYRLRL HFDGYSECHD FWVNANSPDI HPAGWFEKTG
310 320 330 340 350
HKLQPPKGYK EEEFSWSQYL RSTRAQAAPK HLFVSQSHSP PPLGFQVGMK
360 370 380 390 400
LEAVDRMNPS LVCVASVTDV VDSRFLVHFD NWDDTYDYWC DPSSPYIHPV
410 420 430 440 450
GWCQKQGKPL TPPQDYPDPD NFCWEKYLEE TGASAVPTWA FKVRPPHSFL
460 470 480 490 500
VNMKLEAVDR RNPALIRVAS VEDVEDHRIK IHFDGWSHGY DFWIDADHPD
510 520 530 540 550
IHPAGWCSKT GHPLQPPLGP REPSSASPGG CPPLSYRSLP HTRTSKYSFH
560 570 580 590 600
HRKCPTPGCD GSGHVTGKFT AHHCLSGCPL AERNQSRLKA ELSDSEASAR
610 620 630 640 650
KKNLSGFSPR KKPRHHGRIG RPPKYRKIPQ EDFQTLTPDV VHQSLFMSAL
660 670 680 690 700
SAHPDRSLSV CWEQHCKLLP GVAGISASTV AKWTIDEVFG FVQTLTGCED
710 720 730 740 750
QARLFKDEMI DGEAFLLLTQ ADIVKIMSVK LGPALKIYNA ILMFKNADDT

LK
Length:752
Mass (Da):83,884
Last modified:March 8, 2011 - v3
Checksum:i6B92FF852FF98CB4
GO
Isoform 1 (identifier: Q9Y468-1) [UniParc]FASTAAdd to basket

Also known as: mbt-I

The sequence of this isoform differs from the canonical sequence as follows:
     709-752: MIDGEAFLLL...MFKNADDTLK → ARIVRVTHVS...KLSFASDSQY

Show »
Length:772
Mass (Da):85,917
Checksum:i117B03A628826B29
GO
Isoform 2 (identifier: Q9Y468-2) [UniParc]FASTAAdd to basket

Also known as: mbt-II

The sequence of this isoform differs from the canonical sequence as follows:
     709-752: MIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNADDTLK → VRCKCRVGDRAGVTVLKTAGSRCPPQRHFC

Show »
Length:738
Mass (Da):82,318
Checksum:i091F0E829CE6665D
GO
Isoform 3 (identifier: Q9Y468-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-348: Missing.
     709-752: MIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNADDTLK → VRCKCRVGDRAGVTVLKTAGSRCPPQRHFC

Show »
Length:390
Mass (Da):43,766
Checksum:i8C720B89B9DD6388
GO
Isoform 5 (identifier: Q9Y468-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MRRREGHGTDSEMGQGPVRESQSSDPPALQ → MHLVAGDSPG...AAPPPGGGLR
     709-752: MIDGEAFLLL...MFKNADDTLK → ARIVRVTHVS...KLSFASDSQY

Note: No experimental confirmation available.
Show »
Length:840
Mass (Da):92,297
Checksum:i70004D458897CB24
GO

Sequence cautioni

The sequence CAI23042.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI42317.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW75958.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW75961.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW75962.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861T → A in BAG61241 (PubMed:14702039).Curated
Sequence conflicti305 – 3051P → L in AAC69438 (PubMed:10445843).Curated
Sequence conflicti320 – 3212LR → MC in AAC69438 (PubMed:10445843).Curated
Sequence conflicti332 – 3321L → M in AAC69438 (PubMed:10445843).Curated
Sequence conflicti493 – 4931W → R in BAG61241 (PubMed:14702039).Curated
Sequence conflicti595 – 5951S → P in AAC69438 (PubMed:10445843).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491S → T.1 Publication
Corresponds to variant rs17857202 [ dbSNP | Ensembl ].
VAR_051097
Natural varianti479 – 4791I → M.
Corresponds to variant rs6017104 [ dbSNP | Ensembl ].
VAR_051098
Isoform 1 (identifier: Q9Y468-1)
Natural varianti759 – 7591H → R DbSNP:rs6030948.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 348348Missing in isoform 3. 1 PublicationVSP_003901Add
BLAST
Alternative sequencei1 – 3030MRRRE…PPALQ → MHLVAGDSPGSGPHLPATAF IIPASSATLGLPSSALDVSC FPREPIHVGAPEQVAGCEPV SATVLPQLSAGPASSSTSTV RLLEWTEAAAPPPGGGLR in isoform 5. 1 PublicationVSP_040719Add
BLAST
Alternative sequencei709 – 75244MIDGE…DDTLK → ARIVRVTHVSGKTLVWTVAQ LGDLVCSDHLQEGKGILETG VHSLLCSLPTHLLAKLSFAS DSQY in isoform 1 and isoform 5. 3 PublicationsVSP_003903Add
BLAST
Alternative sequencei709 – 75244MIDGE…DDTLK → VRCKCRVGDRAGVTVLKTAG SRCPPQRHFC in isoform 2 and isoform 3. 2 PublicationsVSP_003902Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89358 mRNA. Translation: AAC69438.1.
AK299199 mRNA. Translation: BAG61241.1.
AL110279 mRNA. Translation: CAB53714.1.
AL031681, Z98752 Genomic DNA. Translation: CAI23043.1.
Z98752 Genomic DNA. Translation: CAC16800.1.
Z98752 Genomic DNA. Translation: CAC18508.1.
Z98752, AL031681 Genomic DNA. Translation: CAI42318.1.
AL031681, Z98752 Genomic DNA. Translation: CAI23042.1. Sequence problems.
Z98752, AL031681 Genomic DNA. Translation: CAI42317.1. Sequence problems.
CH471077 Genomic DNA. Translation: EAW75958.1. Sequence problems.
CH471077 Genomic DNA. Translation: EAW75961.1. Sequence problems.
CH471077 Genomic DNA. Translation: EAW75962.1. Sequence problems.
BC039820 mRNA. Translation: AAH39820.1.
AB014581 mRNA. Translation: BAA31656.1.
CCDSiCCDS13319.1. [Q9Y468-1]
CCDS46602.2. [Q9Y468-5]
PIRiT14794.
RefSeqiNP_056293.4. NM_015478.6. [Q9Y468-1]
NP_115479.4. NM_032107.4. [Q9Y468-5]
UniGeneiHs.709356.
Hs.736988.

Genome annotation databases

EnsembliENST00000373135; ENSP00000362227; ENSG00000185513. [Q9Y468-1]
ENST00000418998; ENSP00000398516; ENSG00000185513. [Q9Y468-5]
ENST00000427442; ENSP00000402107; ENSG00000185513. [Q9Y468-5]
GeneIDi26013.
KEGGihsa:26013.
UCSCiuc002xkl.4. human. [Q9Y468-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89358 mRNA. Translation: AAC69438.1.
AK299199 mRNA. Translation: BAG61241.1.
AL110279 mRNA. Translation: CAB53714.1.
AL031681, Z98752 Genomic DNA. Translation: CAI23043.1.
Z98752 Genomic DNA. Translation: CAC16800.1.
Z98752 Genomic DNA. Translation: CAC18508.1.
Z98752, AL031681 Genomic DNA. Translation: CAI42318.1.
AL031681, Z98752 Genomic DNA. Translation: CAI23042.1. Sequence problems.
Z98752, AL031681 Genomic DNA. Translation: CAI42317.1. Sequence problems.
CH471077 Genomic DNA. Translation: EAW75958.1. Sequence problems.
CH471077 Genomic DNA. Translation: EAW75961.1. Sequence problems.
CH471077 Genomic DNA. Translation: EAW75962.1. Sequence problems.
BC039820 mRNA. Translation: AAH39820.1.
AB014581 mRNA. Translation: BAA31656.1.
CCDSiCCDS13319.1. [Q9Y468-1]
CCDS46602.2. [Q9Y468-5]
PIRiT14794.
RefSeqiNP_056293.4. NM_015478.6. [Q9Y468-1]
NP_115479.4. NM_032107.4. [Q9Y468-5]
UniGeneiHs.709356.
Hs.736988.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OYXX-ray1.85A/B/C197-527[»]
1OZ2X-ray1.55A197-527[»]
1OZ3X-ray1.85A/B/C197-527[»]
2PQWX-ray2.00A200-522[»]
2RHIX-ray1.66A197-526[»]
2RHUX-ray1.90A206-519[»]
2RHXX-ray2.10A197-526[»]
2RHYX-ray1.90A206-519[»]
2RHZX-ray2.20A206-519[»]
2RI2X-ray2.20A206-519[»]
2RI3X-ray2.00A206-519[»]
2RI5X-ray2.00A206-519[»]
2RJCX-ray2.00A/B/C200-530[»]
2RJDX-ray1.65A200-530[»]
2RJEX-ray1.86A/B/C200-530[»]
2RJFX-ray2.05A/C/E200-530[»]
3OQ5X-ray2.50A/B/C191-530[»]
3P8HX-ray2.55A/B/C200-522[»]
3UWNX-ray2.15A200-530[»]
ProteinModelPortaliQ9Y468.
SMRiQ9Y468. Positions 204-581, 683-737.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117486. 43 interactions.
DIPiDIP-29628N.
IntActiQ9Y468. 5 interactions.
MINTiMINT-2830196.
STRINGi9606.ENSP00000398516.

Chemistry

BindingDBiQ9Y468.
ChEMBLiCHEMBL1287622.

PTM databases

PhosphoSiteiQ9Y468.

Polymorphism and mutation databases

BioMutaiL3MBTL1.
DMDMi325511398.

Proteomic databases

EPDiQ9Y468.
PaxDbiQ9Y468.
PRIDEiQ9Y468.

Protocols and materials databases

DNASUi26013.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373135; ENSP00000362227; ENSG00000185513. [Q9Y468-1]
ENST00000418998; ENSP00000398516; ENSG00000185513. [Q9Y468-5]
ENST00000427442; ENSP00000402107; ENSG00000185513. [Q9Y468-5]
GeneIDi26013.
KEGGihsa:26013.
UCSCiuc002xkl.4. human. [Q9Y468-4]

Organism-specific databases

CTDi26013.
GeneCardsiL3MBTL1.
H-InvDBHIX0015827.
HGNCiHGNC:15905. L3MBTL1.
MIMi608802. gene.
neXtProtiNX_Q9Y468.
PharmGKBiPA30260.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3766. Eukaryota.
ENOG410Y4AQ. LUCA.
GeneTreeiENSGT00760000119024.
HOVERGENiHBG071375.
InParanoidiQ9Y468.
OMAiQEDFQTI.
OrthoDBiEOG7FR7FT.
PhylomeDBiQ9Y468.
TreeFamiTF316498.

Miscellaneous databases

ChiTaRSiL3MBTL1. human.
EvolutionaryTraceiQ9Y468.
GeneWikiiL3MBTL.
GenomeRNAii26013.
NextBioi47770.
PROiQ9Y468.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y468.
CleanExiHS_L3MBTL.
ExpressionAtlasiQ9Y468. baseline and differential.
GenevisibleiQ9Y468. HS.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR002515. Znf_C2HC.
[Graphical view]
PfamiPF02820. MBT. 3 hits.
PF00536. SAM_1. 1 hit.
PF01530. zf-C2HC. 1 hit.
[Graphical view]
SMARTiSM00561. MBT. 3 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS51079. MBT. 3 hits.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human homolog of Drosophila lethal(3)malignant brain tumor (l(3)mbt) protein associates with condensed mitotic chromosomes."
    Koga H., Matsui S., Hirota T., Takebayashi S., Okumura K., Saya H.
    Oncogene 18:3799-3809(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "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).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Uterus.
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1), VARIANT THR-49.
    Tissue: Brain.
  6. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 215-752 (ISOFORM 4).
    Tissue: Brain.
  7. "The human L(3)MBT Polycomb group protein is a transcriptional repressor and interacts physically and functionally with TEL (ETV6)."
    Boccuni P., MacGrogan D., Scandura J.M., Nimer S.D.
    J. Biol. Chem. 278:15412-15420(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ETV6.
  8. "Imprinting of the human L3MBTL gene, a polycomb family member located in a region of chromosome 20 deleted in human myeloid malignancies."
    Li J., Bench A.J., Vassiliou G.S., Fourouclas N., Ferguson-Smith A.C., Green A.R.
    Proc. Natl. Acad. Sci. U.S.A. 101:7341-7346(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMPRINTING.
  9. Cited for: FUNCTION, INTERACTION WITH CBX3 AND HISTONES, MUTAGENESIS OF ASP-248; PHE-272; ASP-355; PHE-379; ASP-459 AND PHE-483.
  10. "Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1."
    Kalakonda N., Fischle W., Boccuni P., Gurvich N., Hoya-Arias R., Zhao X., Miyata Y., Macgrogan D., Zhang J., Sims J.K., Rice J.C., Nimer S.D.
    Oncogene 27:4293-4304(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KMT5A.
  11. Cited for: FUNCTION, INTERACTION WITH RB1.
  12. "The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks."
    Acs K., Luijsterburg M.S., Ackermann L., Salomons F.A., Hoppe T., Dantuma N.P.
    Nat. Struct. Mol. Biol. 18:1345-1350(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH VCP.
  13. "Malignant brain tumor repeats: a three-leaved propeller architecture with ligand/peptide binding pockets."
    Wang W.K., Tereshko V., Boccuni P., MacGrogan D., Nimer S.D., Patel D.J.
    Structure 11:775-789(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 197-527.
  14. "Structural basis for lower lysine methylation state-specific readout by MBT repeats of L3MBTL1 and an engineered PHD finger."
    Li H., Fischle W., Wang W., Duncan E.M., Liang L., Murakami-Ishibe S., Allis C.D., Patel D.J.
    Mol. Cell 28:677-691(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 206-519 IN COMPLEX WITH MONOMETHYLATED AND DIMETHYLATED PEPTIDES, DOMAIN MBT REPEAT, MUTAGENESIS OF ASP-355 AND ASN-358.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 200-530 IN COMPLEX WITH DIMETHYLATED HISTONE H4, MUTAGENESIS OF ASP-355 AND CYS-363.
  16. Erratum
    Min J., Allali-Hassani A., Nady N., Qi C., Ouyang H., Liu Y., MacKenzie F., Vedadi M., Arrowsmith C.H.
    Nat. Struct. Mol. Biol. 15:114-114(2008)
  17. "The MBT repeats of L3MBTL1 link SET8-mediated p53 methylation at lysine 382 to target gene repression."
    West L.E., Roy S., Lachmi-Weiner K., Hayashi R., Shi X., Appella E., Kutateladze T.G., Gozani O.
    J. Biol. Chem. 285:37725-37732(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 191-530 IN COMPLEX WITH MONOMETHYLATED PEPTIDE, FUNCTION, INTERACTION WITH TP53, MUTAGENESIS OF ASP-355; ASN-358; PHE-379; TRP-382 AND TYR-386.
  18. "Small molecule ligands of methyl-lysine binding proteins."
    Structural genomics consortium (SGC)
    Submitted (NOV-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 200-522.

Entry informationi

Entry nameiLMBL1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y468
Secondary accession number(s): B4DRC9
, E1P5W7, Q5H8Y8, Q5H8Y9, Q8IUV7, Q9H1E6, Q9H1G5, Q9UG06, Q9UJB9, Q9Y4C9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 8, 2011
Last modified: May 11, 2016
This is version 167 of the entry and version 3 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

Miscellaneous

The L3MBTL1 locus is imprinted. Paternal inherited gene is expressed, while the maternal inherited gene is silenced.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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.