Q9Y468 (LMBL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	L3MBTL1
Synonyms:	KIAA0681, L3MBT, L3MBTL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	752 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9 Ref.10 Ref.11 Ref.16
Subunit structure	Homodimer. Interacts with RB1/RB (when monomethylated at 'Lys-860'). Interacts with p53/TP53 (when monomethylated at 'Lys-382'). Interacts with CBX3, ETV6 and SETD8. Ref.7 Ref.9 Ref.10 Ref.11 Ref.16
Subcellular location	Nucleus. 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. Ref.1
Tissue specificity	Widely expressed. Expression is reduced in colorectal cancer cell line SW480 and promyelocytic leukemia cell line HL-60. Ref.1
Developmental stage	In interphase cells, it is scattered throughout the nucleoplasm. In mitotic cells, it strongly associates with condensed chromosomes from the prophase to telophase.
Domain	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. Ref.13
Miscellaneous	The L3MBTL1 locus is imprinted. Paternal inherited gene is expressed, while the maternal inherited gene is silenced.
Sequence similarities	Contains 1 C2HC-type zinc finger. Contains 3 MBT repeats. Contains 1 SAM (sterile alpha motif) domain.
Sequence caution	The sequence CAI23042.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI42317.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAW75958.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAW75961.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAW75962.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from direct assay Ref.9. Source: UniProtKB hemopoiesis Inferred from expression pattern. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.9Ref.10. Source: UniProtKB regulation of megakaryocyte differentiation Inferred from direct assay. Source: UniProtKB regulation of mitosis Inferred from mutant phenotype Ref.1. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin Inferred from direct assay Ref.10. Source: UniProtKB condensed chromosome Inferred from direct assay Ref.1. Source: UniProtKB nucleoplasm Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	SAM domain binding Inferred from physical interaction Ref.7. Source: UniProtKB identical protein binding Inferred from physical interaction Ref.7. Source: UniProtKB methylated histone residue binding Inferred from direct assay. Source: UniProtKB nucleosomal histone binding Inferred from direct assay Ref.9. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HIST1H1E	P10412	7	EBI-1265089,EBI-358163
HIST1H4A	P62805	3	EBI-1265089,EBI-302023

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: Q9Y468-4) 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 1 (identifier: Q9Y468-1) Also known as: mbt-I; The sequence of this isoform differs from the canonical sequence as follows:      709-752: MIDGEAFLLL...MFKNADDTLK → ARIVRVTHVS...KLSFASDSQY
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Natural variant	759	1	H → R DbSNP:rs6030948.
Isoform 2 (identifier: Q9Y468-2) Also known as: mbt-II; The sequence of this isoform differs from the canonical sequence as follows:      709-752: MIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNADDTLK → VRCKCRVGDRAGVTVLKTAGSRCPPQRHFC
Isoform 3 (identifier: Q9Y468-3) The sequence of this isoform differs from the canonical sequence as follows:      1-348: Missing.      709-752: MIDGEAFLLLTQADIVKIMSVKLGPALKIYNAILMFKNADDTLK → VRCKCRVGDRAGVTVLKTAGSRCPPQRHFC
Isoform 5 (identifier: Q9Y468-5) 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 752

752

Lethal(3)malignant brain tumor-like protein 1

PRO_0000084452

Regions

Repeat

206 – 306

101

MBT 1

Repeat

314 – 413

100

MBT 2

Repeat

422 – 517

96

MBT 3

Domain

683 – 747

65

SAM

Zinc finger

552 – 578

27

C2HC-type

Region

379 – 386

8

Interaction with monomethylated and dimethylated peptides

Sites

Site

355

1

Mediates recognition of monomethylated and dimethylated peptides

Site

358

1

positioned at the entrance of MBT 2 and is required for recognition of monomethylated and dimethylated peptides

Natural variations

Alternative sequence

1 – 348

348

Missing in isoform 3.

VSP_003901

Alternative sequence

1 – 30

30

MRRRE…PPALQ → MHLVAGDSPGSGPHLPATAF IIPASSATLGLPSSALDVSC FPREPIHVGAPEQVAGCEPV SATVLPQLSAGPASSSTSTV RLLEWTEAAAPPPGGGLR in isoform 5.

VSP_040719

Alternative sequence

709 – 752

44

MIDGE…DDTLK → ARIVRVTHVSGKTLVWTVAQ LGDLVCSDHLQEGKGILETG VHSLLCSLPTHLLAKLSFAS DSQY in isoform 1 and isoform 5.

VSP_003903

Alternative sequence

709 – 752

44

MIDGE…DDTLK → VRCKCRVGDRAGVTVLKTAG SRCPPQRHFC in isoform 2 and isoform 3.

VSP_003902

Natural variant

49

1

S → T. Ref.5
Corresponds to variant rs17857202 [ dbSNP | Ensembl ].

VAR_051097

Natural variant

479

1

I → M.
Corresponds to variant rs6017104 [ dbSNP | Ensembl ].

VAR_051098

Experimental info

Mutagenesis

248

1

D → N: Does not affect binding to monomethylated and dimethylated peptides. Ref.9

Mutagenesis

272

1

F → A: Does not affect binding to monomethylated and dimethylated peptides. Ref.9

Mutagenesis

355

1

D → A: Abolishes binding to monomethylated and dimethylated peptides. Ref.9 Ref.13 Ref.14 Ref.16

Mutagenesis

355

1

D → N: Strongly impairs binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. Ref.9 Ref.13 Ref.14 Ref.16

Mutagenesis

358

1

N → A: Abolishes binding to monomethylated and dimethylated peptides. Ref.13 Ref.16

Mutagenesis

358

1

N → Q: Strongly impairs binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. Ref.13 Ref.16

Mutagenesis

363

1

C → F or R: Strongly impairs binding to monomethylated and dimethylated peptides. Ref.14

Mutagenesis

379

1

F → A: Abolishes binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. Ref.9 Ref.16

Mutagenesis

382

1

W → L: Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. Ref.16

Mutagenesis

386

1

Y → L: Abolishes binding to p53/TP53 monomethylated at 'Lys-382'. Ref.16

Mutagenesis

459

1

D → N: Does not affect binding to monomethylated and dimethylated peptides. Ref.9

Mutagenesis

483

1

F → A: Does not affect binding to monomethylated and dimethylated peptides. Ref.9

Sequence conflict

186

1

T → A in BAG61241. Ref.2

Sequence conflict

305

1

P → L in AAC69438. Ref.1

Sequence conflict

320 – 321

2

LR → MC in AAC69438. Ref.1

Sequence conflict

332

1

L → M in AAC69438. Ref.1

Sequence conflict

493

1

W → R in BAG61241. Ref.2

Sequence conflict

595

1

S → P in AAC69438. Ref.1

Secondary structure

1

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752

Helix Strand Turn

Details...

Helix

208 – 215

8

Helix

222 – 224

3

Helix

227 – 230

4

Beta strand

243 – 248

6

Beta strand

251 – 264

14

Beta strand

267 – 272

6

Helix

277 – 279

3

Beta strand

281 – 284

4

Helix

295 – 299

5

Helix

311 – 313

3

Helix

316 – 323

8

Helix

330 – 332

3

Beta strand

350 – 354

5

Beta strand

362 – 371

10

Beta strand

374 – 379

6

Helix

384 – 386

3

Beta strand

388 – 390

3

Helix

402 – 406

5

Helix

424 – 430

7

Helix

438 – 440

3

Beta strand

454 – 458

5

Beta strand

466 – 474

9

Beta strand

476 – 483

8

Helix

488 – 490

3

Beta strand

492 – 495

4

Helix

506 – 510

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 4 [UniParc]. Last modified March 8, 2011. Version 3. Checksum: 6B92FF852FF98CB4	FASTA	752	83,884
	10 20 30 40 50 60 MRRREGHGTD SEMGQGPVRE SQSSDPPALQ FRISEYKPLN MAGVEQPPSP ELRQEGVTEY 70 80 90 100 110 120 EDGGAPAGDG EAGPQQAEDH PQNPPEDPNQ DPPEDDSTCQ CQACGPHQAA GPDLGSSNDG 130 140 150 160 170 180 CPQLFQERSV IVENSSGSTS ASELLKPMKK RKRREYQSPS EEESEPEAME KQEEGKDPEG 190 200 210 220 230 240 QPTASTPESE EWSSSQPATG EKKECWSWES YLEEQKAITA PVSLFQDSQA VTHNKNGFKL 250 260 270 280 290 300 GMKLEGIDPQ HPSMYFILTV AEVCGYRLRL HFDGYSECHD FWVNANSPDI HPAGWFEKTG 310 320 330 340 350 360 HKLQPPKGYK EEEFSWSQYL RSTRAQAAPK HLFVSQSHSP PPLGFQVGMK LEAVDRMNPS 370 380 390 400 410 420 LVCVASVTDV VDSRFLVHFD NWDDTYDYWC DPSSPYIHPV GWCQKQGKPL TPPQDYPDPD 430 440 450 460 470 480 NFCWEKYLEE TGASAVPTWA FKVRPPHSFL VNMKLEAVDR RNPALIRVAS VEDVEDHRIK 490 500 510 520 530 540 IHFDGWSHGY DFWIDADHPD IHPAGWCSKT GHPLQPPLGP REPSSASPGG CPPLSYRSLP 550 560 570 580 590 600 HTRTSKYSFH HRKCPTPGCD GSGHVTGKFT AHHCLSGCPL AERNQSRLKA ELSDSEASAR 610 620 630 640 650 660 KKNLSGFSPR KKPRHHGRIG RPPKYRKIPQ EDFQTLTPDV VHQSLFMSAL SAHPDRSLSV 670 680 690 700 710 720 CWEQHCKLLP GVAGISASTV AKWTIDEVFG FVQTLTGCED QARLFKDEMI DGEAFLLLTQ 730 740 750 ADIVKIMSVK LGPALKIYNA ILMFKNADDT LK
	Isoform 1 (mbt-I) [UniParc]. Checksum: 117B03A628826B29	FASTA	772	85,917
	10 20 30 40 50 60 MRRREGHGTD SEMGQGPVRE SQSSDPPALQ FRISEYKPLN MAGVEQPPSP ELRQEGVTEY 70 80 90 100 110 120 EDGGAPAGDG EAGPQQAEDH PQNPPEDPNQ DPPEDDSTCQ CQACGPHQAA GPDLGSSNDG 130 140 150 160 170 180 CPQLFQERSV IVENSSGSTS ASELLKPMKK RKRREYQSPS EEESEPEAME KQEEGKDPEG 190 200 210 220 230 240 QPTASTPESE EWSSSQPATG EKKECWSWES YLEEQKAITA PVSLFQDSQA VTHNKNGFKL 250 260 270 280 290 300 GMKLEGIDPQ HPSMYFILTV AEVCGYRLRL HFDGYSECHD FWVNANSPDI HPAGWFEKTG 310 320 330 340 350 360 HKLQPPKGYK EEEFSWSQYL RSTRAQAAPK HLFVSQSHSP PPLGFQVGMK LEAVDRMNPS 370 380 390 400 410 420 LVCVASVTDV VDSRFLVHFD NWDDTYDYWC DPSSPYIHPV GWCQKQGKPL TPPQDYPDPD 430 440 450 460 470 480 NFCWEKYLEE TGASAVPTWA FKVRPPHSFL VNMKLEAVDR RNPALIRVAS VEDVEDHRIK 490 500 510 520 530 540 IHFDGWSHGY DFWIDADHPD IHPAGWCSKT GHPLQPPLGP REPSSASPGG CPPLSYRSLP 550 560 570 580 590 600 HTRTSKYSFH HRKCPTPGCD GSGHVTGKFT AHHCLSGCPL AERNQSRLKA ELSDSEASAR 610 620 630 640 650 660 KKNLSGFSPR KKPRHHGRIG RPPKYRKIPQ EDFQTLTPDV VHQSLFMSAL SAHPDRSLSV 670 680 690 700 710 720 CWEQHCKLLP GVAGISASTV AKWTIDEVFG FVQTLTGCED QARLFKDEAR IVRVTHVSGK 730 740 750 760 770 TLVWTVAQLG DLVCSDHLQE GKGILETGVH SLLCSLPTHL LAKLSFASDS QY
	Isoform 2 (mbt-II) [UniParc]. Checksum: 091F0E829CE6665D	FASTA	738	82,318
	10 20 30 40 50 60 MRRREGHGTD SEMGQGPVRE SQSSDPPALQ FRISEYKPLN MAGVEQPPSP ELRQEGVTEY 70 80 90 100 110 120 EDGGAPAGDG EAGPQQAEDH PQNPPEDPNQ DPPEDDSTCQ CQACGPHQAA GPDLGSSNDG 130 140 150 160 170 180 CPQLFQERSV IVENSSGSTS ASELLKPMKK RKRREYQSPS EEESEPEAME KQEEGKDPEG 190 200 210 220 230 240 QPTASTPESE EWSSSQPATG EKKECWSWES YLEEQKAITA PVSLFQDSQA VTHNKNGFKL 250 260 270 280 290 300 GMKLEGIDPQ HPSMYFILTV AEVCGYRLRL HFDGYSECHD FWVNANSPDI HPAGWFEKTG 310 320 330 340 350 360 HKLQPPKGYK EEEFSWSQYL RSTRAQAAPK HLFVSQSHSP PPLGFQVGMK LEAVDRMNPS 370 380 390 400 410 420 LVCVASVTDV VDSRFLVHFD NWDDTYDYWC DPSSPYIHPV GWCQKQGKPL TPPQDYPDPD 430 440 450 460 470 480 NFCWEKYLEE TGASAVPTWA FKVRPPHSFL VNMKLEAVDR RNPALIRVAS VEDVEDHRIK 490 500 510 520 530 540 IHFDGWSHGY DFWIDADHPD IHPAGWCSKT GHPLQPPLGP REPSSASPGG CPPLSYRSLP 550 560 570 580 590 600 HTRTSKYSFH HRKCPTPGCD GSGHVTGKFT AHHCLSGCPL AERNQSRLKA ELSDSEASAR 610 620 630 640 650 660 KKNLSGFSPR KKPRHHGRIG RPPKYRKIPQ EDFQTLTPDV VHQSLFMSAL SAHPDRSLSV 670 680 690 700 710 720 CWEQHCKLLP GVAGISASTV AKWTIDEVFG FVQTLTGCED QARLFKDEVR CKCRVGDRAG 730 VTVLKTAGSR CPPQRHFC
	Isoform 3 [UniParc]. Checksum: 8C720B89B9DD6388	FASTA	390	43,766
	10 20 30 40 50 60 MKLEAVDRMN PSLVCVASVT DVVDSRFLVH FDNWDDTYDY WCDPSSPYIH PVGWCQKQGK 70 80 90 100 110 120 PLTPPQDYPD PDNFCWEKYL EETGASAVPT WAFKVRPPHS FLVNMKLEAV DRRNPALIRV 130 140 150 160 170 180 ASVEDVEDHR IKIHFDGWSH GYDFWIDADH PDIHPAGWCS KTGHPLQPPL GPREPSSASP 190 200 210 220 230 240 GGCPPLSYRS LPHTRTSKYS FHHRKCPTPG CDGSGHVTGK FTAHHCLSGC PLAERNQSRL 250 260 270 280 290 300 KAELSDSEAS ARKKNLSGFS PRKKPRHHGR IGRPPKYRKI PQEDFQTLTP DVVHQSLFMS 310 320 330 340 350 360 ALSAHPDRSL SVCWEQHCKL LPGVAGISAS TVAKWTIDEV FGFVQTLTGC EDQARLFKDE 370 380 390 VRCKCRVGDR AGVTVLKTAG SRCPPQRHFC
	Isoform 5 [UniParc]. Checksum: 70004D458897CB24	FASTA	840	92,297
	10 20 30 40 50 60 MHLVAGDSPG SGPHLPATAF IIPASSATLG LPSSALDVSC FPREPIHVGA PEQVAGCEPV 70 80 90 100 110 120 SATVLPQLSA GPASSSTSTV RLLEWTEAAA PPPGGGLRFR ISEYKPLNMA GVEQPPSPEL 130 140 150 160 170 180 RQEGVTEYED GGAPAGDGEA GPQQAEDHPQ NPPEDPNQDP PEDDSTCQCQ ACGPHQAAGP 190 200 210 220 230 240 DLGSSNDGCP QLFQERSVIV ENSSGSTSAS ELLKPMKKRK RREYQSPSEE ESEPEAMEKQ 250 260 270 280 290 300 EEGKDPEGQP TASTPESEEW SSSQPATGEK KECWSWESYL EEQKAITAPV SLFQDSQAVT 310 320 330 340 350 360 HNKNGFKLGM KLEGIDPQHP SMYFILTVAE VCGYRLRLHF DGYSECHDFW VNANSPDIHP 370 380 390 400 410 420 AGWFEKTGHK LQPPKGYKEE EFSWSQYLRS TRAQAAPKHL FVSQSHSPPP LGFQVGMKLE 430 440 450 460 470 480 AVDRMNPSLV CVASVTDVVD SRFLVHFDNW DDTYDYWCDP SSPYIHPVGW CQKQGKPLTP 490 500 510 520 530 540 PQDYPDPDNF CWEKYLEETG ASAVPTWAFK VRPPHSFLVN MKLEAVDRRN PALIRVASVE 550 560 570 580 590 600 DVEDHRIKIH FDGWSHGYDF WIDADHPDIH PAGWCSKTGH PLQPPLGPRE PSSASPGGCP 610 620 630 640 650 660 PLSYRSLPHT RTSKYSFHHR KCPTPGCDGS GHVTGKFTAH HCLSGCPLAE RNQSRLKAEL 670 680 690 700 710 720 SDSEASARKK NLSGFSPRKK PRHHGRIGRP PKYRKIPQED FQTLTPDVVH QSLFMSALSA 730 740 750 760 770 780 HPDRSLSVCW EQHCKLLPGV AGISASTVAK WTIDEVFGFV QTLTGCEDQA RLFKDEARIV 790 800 810 820 830 840 RVTHVSGKTL VWTVAQLGDL VCSDHLQEGK GILETGVHSL LCSLPTHLLA KLSFASDSQY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10445843] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] 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: 11780052] [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: 15489334] [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: 9734811] [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: 12588862] [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: 15123827] [Abstract] Cited for: IMPRINTING.
[9]	"L3MBTL1, a histone-methylation-dependent chromatin lock." Trojer P., Li G., Sims R.J. III, Vaquero A., Kalakonda N., Boccuni P., Lee D., Erdjument-Bromage H., Tempst P., Nimer S.D., Wang Y.H., Reinberg D. Cell 129:915-928(2007) [PubMed: 17540172] [Abstract] 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: 18408754] [Abstract] Cited for: FUNCTION, INTERACTION WITH SETD8.
[11]	"Methylation of the retinoblastoma tumor suppressor by SMYD2." Saddic L.A., West L.E., Aslanian A., Yates J.R. III, Rubin S.M., Gozani O., Sage J. J. Biol. Chem. 285:37733-37740(2010) [PubMed: 20870719] [Abstract] Cited for: FUNCTION, INTERACTION WITH RB1.
[12]	"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: 12842041] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 197-527.
[13]	"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: 18042461] [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.
[14]	"L3MBTL1 recognition of mono- and dimethylated histones." Min J., Allali-Hassani A., Nady N., Qi C., Ouyang H., Liu Y., MacKenzie F., Vedadi M., Arrowsmith C.H. Nat. Struct. Mol. Biol. 14:1229-1230(2007) [PubMed: 18026117] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 200-530 IN COMPLEX WITH DIMETHYLATED HISTONE H4, MUTAGENESIS OF ASP-355 AND CYS-363.
[15]	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)
[16]	"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: 20870725] [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.
[17]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00216288.
IPI00216289.
IPI00333371.
IPI00879524.
IPI00971010.

PIR

T14794.

RefSeq

NP_056293.4. NM_015478.6.
NP_115479.4. NM_032107.4.

UniGene

Hs.709356.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OYX	X-ray	1.85	A/B/C	197-527	[»]
1OZ2	X-ray	1.55	A	197-527	[»]
1OZ3	X-ray	1.85	A/B/C	197-527	[»]
2PQW	X-ray	2.00	A	200-522	[»]
2RHI	X-ray	1.66	A	197-526	[»]
2RHU	X-ray	1.90	A	206-519	[»]
2RHX	X-ray	2.10	A	197-526	[»]
2RHY	X-ray	1.90	A	206-519	[»]
2RHZ	X-ray	2.20	A	206-519	[»]
2RI2	X-ray	2.20	A	206-519	[»]
2RI3	X-ray	2.00	A	206-519	[»]
2RI5	X-ray	2.00	A	206-519	[»]
2RJC	X-ray	2.00	A/B/C	200-530	[»]
2RJD	X-ray	1.65	A	200-530	[»]
2RJE	X-ray	1.86	A/B/C	200-530	[»]
2RJF	X-ray	2.05	A/C/E	200-530	[»]
3OQ5	X-ray	2.50	A/B/C	191-530	[»]
3P8H	X-ray	2.55	A/B/C	200-522	[»]

ProteinModelPortal

Q9Y468.

SMR

Q9Y468. Positions 204-590, 677-745.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29628N.

IntAct

Q9Y468. 4 interactions.

MINT

MINT-2830196.

STRING

Q9Y468.

PTM databases

PhosphoSite

Q9Y468.

Polymorphism databases

DMDM

23396689.

Proteomic databases

PRIDE

Q9Y468.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373134; ENSP00000362226; ENSG00000185513.
ENST00000373135; ENSP00000362227; ENSG00000185513.

GeneID

26013.

KEGG

hsa:26013.

UCSC

uc002xkl.1. human.
uc002xkm.1. human.

Organism-specific databases

CTD

26013.

GeneCards

GC20P042137.

HGNC

HGNC:15905. L3MBTL1.

MIM

608802. gene.

neXtProt

NX_Q9Y468.

PharmGKB

PA30260.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00560000076796.

HOVERGEN

HBG071375.

InParanoid

Q9Y468.

OMA

EMIDGEA.

OrthoDB

EOG46MBJH.

Gene expression databases

ArrayExpress

Q9Y468.

Bgee

Q9Y468.

CleanEx

HS_L3MBTL.

Genevestigator

Q9Y468.

GermOnline

ENSG00000185513. Homo sapiens.

Family and domain databases

InterPro

IPR004092. Mbt.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR002515. Znf_C2HC.
[Graphical view]

Gene3D

G3DSA:1.10.150.50. SAM_type. 1 hit.

Pfam

PF02820. MBT. 3 hits.
PF00536. SAM_1. 1 hit.
PF01530. zf-C2HC. 1 hit.
[Graphical view]

SMART

SM00561. MBT. 3 hits.
SM00454. SAM. 1 hit.
[Graphical view]

SUPFAM

SSF47769. SAM_homology. 1 hit.

PROSITE

PS51079. MBT. 3 hits.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

47770.

SOURCE

Search...

Entry information

Entry name

LMBL1_HUMAN

Accession

Primary (citable) accession number: Q9Y468
Secondary accession number(s): B4DRC9 , E1P5W7, Q5H8Y8, Q5H8Y9, Q8IUV7, Q9H1E6, Q9H1G5, Q9UG06, Q9UJB9, Q9Y4C9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	March 8, 2011
Last modified:	January 25, 2012
This is version 120 of the entry and version 3 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.