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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)DescriptionActionsGraphical viewLength
Sitei355Mediates recognition of monomethylated and dimethylated peptides1
Sitei358Positioned at the entrance of MBT 2 and is required for recognition of monomethylated and dimethylated peptides1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri545 – 588CCHHC-typePROSITE-ProRule annotationAdd BLAST44

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-KW
  • chromatin organization 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
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • 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

Enzyme and pathway databases

BioCyciZFISH:G66-32444-MONOMER.
ReactomeiR-HSA-6804760. Regulation of TP53 Activity through Methylation.

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)DescriptionActionsGraphical viewLength
Mutagenesisi248D → N: Does not affect binding to monomethylated and dimethylated peptides. 1 Publication1
Mutagenesisi272F → A: Does not affect binding to monomethylated and dimethylated peptides. 1 Publication1
Mutagenesisi355D → A: Abolishes binding to monomethylated and dimethylated peptides. 4 Publications1
Mutagenesisi355D → N: Strongly impairs binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. 4 Publications1
Mutagenesisi358N → A: Abolishes binding to monomethylated and dimethylated peptides. 2 Publications1
Mutagenesisi358N → Q: Strongly impairs binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. 2 Publications1
Mutagenesisi363C → F or R: Strongly impairs binding to monomethylated and dimethylated peptides. 1 Publication1
Mutagenesisi379F → A: Abolishes binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. 2 Publications1
Mutagenesisi382W → L: Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. 1 Publication1
Mutagenesisi386Y → L: Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. 1 Publication1
Mutagenesisi459D → N: Does not affect binding to monomethylated and dimethylated peptides. 1 Publication1
Mutagenesisi483F → A: Does not affect binding to monomethylated and dimethylated peptides. 1 Publication1

Organism-specific databases

DisGeNETi26013.
OpenTargetsiENSG00000185513.
PharmGKBiPA30260.

Chemistry databases

ChEMBLiCHEMBL1287622.

Polymorphism and mutation databases

BioMutaiL3MBTL1.
DMDMi325511398.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000844521 – 752Lethal(3)malignant brain tumor-like protein 1Add BLAST752

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei49PhosphoserineCombined sources1

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

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9Y468.
PeptideAtlasiQ9Y468.
PRIDEiQ9Y468.

PTM databases

iPTMnetiQ9Y468.
PhosphoSitePlusiQ9Y468.

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

BgeeiENSG00000185513.
CleanExiHS_L3MBTL.
ExpressionAtlasiQ9Y468. baseline and differential.
GenevisibleiQ9Y468. HS.

Organism-specific databases

HPAiHPA056389.

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
HIST1H3DP684312EBI-1265089,EBI-79722
HIST2H4BP628054EBI-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
  • SAM domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117486. 43 interactors.
DIPiDIP-29628N.
IntActiQ9Y468. 55 interactors.
MINTiMINT-2830196.
STRINGi9606.ENSP00000398516.

Chemistry databases

BindingDBiQ9Y468.

Structurei

Secondary structure

1752
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi208 – 215Combined sources8
Helixi222 – 224Combined sources3
Helixi227 – 230Combined sources4
Beta strandi243 – 248Combined sources6
Beta strandi251 – 264Combined sources14
Beta strandi267 – 272Combined sources6
Helixi277 – 279Combined sources3
Beta strandi281 – 284Combined sources4
Beta strandi288 – 291Combined sources4
Helixi295 – 299Combined sources5
Helixi311 – 313Combined sources3
Helixi316 – 323Combined sources8
Helixi330 – 332Combined sources3
Beta strandi350 – 354Combined sources5
Turni356 – 359Combined sources4
Beta strandi362 – 371Combined sources10
Beta strandi374 – 379Combined sources6
Helixi384 – 386Combined sources3
Beta strandi388 – 390Combined sources3
Helixi402 – 406Combined sources5
Helixi419 – 421Combined sources3
Helixi424 – 431Combined sources8
Helixi438 – 440Combined sources3
Beta strandi454 – 458Combined sources5
Beta strandi460 – 462Combined sources3
Beta strandi466 – 474Combined sources9
Beta strandi476 – 483Combined sources8
Helixi488 – 490Combined sources3
Beta strandi492 – 495Combined sources4
Helixi506 – 510Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y468.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati206 – 306MBT 1Add BLAST101
Repeati314 – 413MBT 2Add BLAST100
Repeati422 – 517MBT 3Add BLAST96
Domaini683 – 747SAMPROSITE-ProRule annotationAdd BLAST65

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni379 – 386Interaction with monomethylated and dimethylated peptides8

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri545 – 588CCHHC-typePROSITE-ProRule annotationAdd BLAST44

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG3766. Eukaryota.
ENOG410Y4AQ. LUCA.
GeneTreeiENSGT00760000119024.
HOVERGENiHBG071375.
InParanoidiQ9Y468.
OMAiQEDFQTI.
OrthoDBiEOG091G01BW.
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.
PS51802. ZF_CCHHC. 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 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI42317 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAW75958 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAW75961 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAW75962 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti186T → A in BAG61241 (PubMed:14702039).Curated1
Sequence conflicti305P → L in AAC69438 (PubMed:10445843).Curated1
Sequence conflicti320 – 321LR → MC in AAC69438 (PubMed:10445843).Curated2
Sequence conflicti332L → M in AAC69438 (PubMed:10445843).Curated1
Sequence conflicti493W → R in BAG61241 (PubMed:14702039).Curated1
Sequence conflicti595S → P in AAC69438 (PubMed:10445843).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05109749S → T.1 PublicationCorresponds to variant rs17857202dbSNPEnsembl.1
Natural variantiVAR_051098479I → M.Corresponds to variant rs6017104dbSNPEnsembl.1
Isoform 1 (identifier: Q9Y468-1)
Natural varianti759H → R DbSNP:rs6030948. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0039011 – 348Missing in isoform 3. 1 PublicationAdd BLAST348
Alternative sequenceiVSP_0407191 – 30MRRRE…PPALQ → MHLVAGDSPGSGPHLPATAF IIPASSATLGLPSSALDVSC FPREPIHVGAPEQVAGCEPV SATVLPQLSAGPASSSTSTV RLLEWTEAAAPPPGGGLR in isoform 5. 1 PublicationAdd BLAST30
Alternative sequenceiVSP_003903709 – 752MIDGE…DDTLK → ARIVRVTHVSGKTLVWTVAQ LGDLVCSDHLQEGKGILETG VHSLLCSLPTHLLAKLSFAS DSQY in isoform 1 and isoform 5. 3 PublicationsAdd BLAST44
Alternative sequenceiVSP_003902709 – 752MIDGE…DDTLK → VRCKCRVGDRAGVTVLKTAG SRCPPQRHFC in isoform 2 and isoform 3. 2 PublicationsAdd BLAST44

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117486. 43 interactors.
DIPiDIP-29628N.
IntActiQ9Y468. 55 interactors.
MINTiMINT-2830196.
STRINGi9606.ENSP00000398516.

Chemistry databases

BindingDBiQ9Y468.
ChEMBLiCHEMBL1287622.

PTM databases

iPTMnetiQ9Y468.
PhosphoSitePlusiQ9Y468.

Polymorphism and mutation databases

BioMutaiL3MBTL1.
DMDMi325511398.

Proteomic databases

PaxDbiQ9Y468.
PeptideAtlasiQ9Y468.
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.
DisGeNETi26013.
GeneCardsiL3MBTL1.
H-InvDBHIX0015827.
HGNCiHGNC:15905. L3MBTL1.
HPAiHPA056389.
MIMi608802. gene.
neXtProtiNX_Q9Y468.
OpenTargetsiENSG00000185513.
PharmGKBiPA30260.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3766. Eukaryota.
ENOG410Y4AQ. LUCA.
GeneTreeiENSGT00760000119024.
HOVERGENiHBG071375.
InParanoidiQ9Y468.
OMAiQEDFQTI.
OrthoDBiEOG091G01BW.
PhylomeDBiQ9Y468.
TreeFamiTF316498.

Enzyme and pathway databases

BioCyciZFISH:G66-32444-MONOMER.
ReactomeiR-HSA-6804760. Regulation of TP53 Activity through Methylation.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000185513.
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.
PS51802. ZF_CCHHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 173 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.