Q969R5 (LMBL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lethal(3)malignant brain tumor-like protein 2
Short name=H-l(3)mbt-like protein 2
Short name=L(3)mbt-like protein 2

Gene names

Name:

L3MBTL2

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	705 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. Ref.12
Subunit structure	Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, BAT8 and YAF2.
Subcellular location	Nucleus Probable.
Sequence similarities	Contains 1 FCS-type zinc finger. Contains 4 MBT repeats.
Sequence caution	The sequence BAB84917.1 differs from that shown. Reason: Intron retention. The sequence BAC04936.1 differs from that shown. Reason: Intron retention.

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
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Non-traceable author statement. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Non-traceable author statement. Source: UniProtKB
Molecular function	methylated histone residue binding Inferred from direct assay Ref.12. Source: UniProtKB transcription corepressor activity Non-traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q969R5-1)

Also known as: A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q969R5-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     608-614: EPATPLK → GKLPRSL
     615-705: Missing.

Isoform 3 (identifier: Q969R5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     608-617: EPATPLKAKE → GVGSRGPKRL
     618-705: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 705

705

Lethal(3)malignant brain tumor-like protein 2

PRO_0000084448

Regions

Repeat

179 – 283

105

MBT 1

Repeat

291 – 391

101

MBT 2

Repeat

397 – 500

104

MBT 3

Repeat

508 – 604

97

MBT 4

Zinc finger

81 – 116

36

FCS-type

Compositional bias

17 – 20

4

Poly-Glu

Compositional bias

620 – 624

5

Poly-Lys

Amino acid modifications

Modified residue

12

1

Phosphoserine Ref.9

Modified residue

13

1

Phosphoserine Ref.9

Modified residue

66

1

Phosphothreonine Ref.8

Modified residue

76

1

Phosphothreonine Ref.8 Ref.11

Modified residue

683

1

Phosphoserine Ref.9

Modified residue

688

1

Phosphoserine Ref.9

Modified residue

689

1

Phosphoserine Ref.9 Ref.10

Natural variations

Alternative sequence

608 – 617

10

EPATPLKAKE → GVGSRGPKRL in isoform 3.

VSP_003906

Alternative sequence

608 – 614

7

EPATPLK → GKLPRSL in isoform 2.

VSP_003904

Alternative sequence

615 – 705

91

Missing in isoform 2.

VSP_003905

Alternative sequence

618 – 705

88

Missing in isoform 3.

VSP_003907

Natural variant

7

1

I → V.
Corresponds to variant rs3804097 [ dbSNP | Ensembl ].

VAR_033998

Natural variant

300

1

R → W.
Corresponds to variant rs2277846 [ dbSNP | Ensembl ].

VAR_015093

Natural variant

337

1

V → A.
Corresponds to variant rs34289721 [ dbSNP | Ensembl ].

VAR_061675

Secondary structure

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705

Helix Strand Turn

Details...

Helix

181 – 188

8

Helix

195 – 197

3

Helix

204 – 206

3

Beta strand

215 – 219

5

Beta strand

230 – 239

10

Beta strand

242 – 247

6

Beta strand

258 – 261

4

Helix

272 – 275

4

Turn

284 – 288

5

Helix

293 – 301

9

Helix

311 – 318

8

Beta strand

328 – 333

6

Beta strand

336 – 349

14

Beta strand

352 – 357

6

Beta strand

365 – 369

5

Helix

380 – 384

5

Helix

412 – 414

3

Beta strand

433 – 438

6

Beta strand

441 – 453

13

Helix

455 – 457

3

Beta strand

458 – 463

6

Beta strand

475 – 478

4

Beta strand

482 – 486

5

Helix

489 – 493

5

Helix

510 – 516

7

Helix

524 – 526

3

Beta strand

541 – 545

5

Beta strand

553 – 562

10

Beta strand

565 – 570

6

Helix

575 – 577

3

Beta strand

579 – 582

4

Helix

593 – 597

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 8FC86A440982FFA7	FASTA	705	79,110
	10 20 30 40 50 60 MEKPRSIEET PSSEPMEEEE DDDLELFGGY DSFRSYNSSV GSESSSYLEE SSEAENEDRE 70 80 90 100 110 120 AGELPTSPLH LLSPGTPRSL DGSGSEPAVC EMCGIVGTRE AFFSKTKRFC SVSCSRSYSS 130 140 150 160 170 180 NSKKASILAR LQGKPPTKKA KVLHKAAWSA KIGAFLHSQG TGQLADGTPT GQDALVLGFD 190 200 210 220 230 240 WGKFLKDHSY KAAPVSCFKH VPLYDQWEDV MKGMKVEVLN SDAVLPSRVY WIASVIQTAG 250 260 270 280 290 300 YRVLLRYEGF ENDASHDFWC NLGTVDVHPI GWCAINSKIL VPPRTIHAKF TDWKGYLMKR 310 320 330 340 350 360 LVGSRTLPVD FHIKMVESMK YPFRQGMRLE VVDKSQVSRT RMAVVDTVIG GRLRLLYEDG 370 380 390 400 410 420 DSDDDFWCHM WSPLIHPVGW SRRVGHGIKM SERRSDMAHH PTFRKIYCDA VPYLFKKVRA 430 440 450 460 470 480 VYTEGGWFEE GMKLEAIDPL NLGNICVATV CKVLLDGYLM ICVDGGPSTD GLDWFCYHAS 490 500 510 520 530 540 SHAIFPATFC QKNDIELTPP KGYEAQTFNW ENYLEKTKSK AAPSRLFNMD CPNHGFKVGM 550 560 570 580 590 600 KLEAVDLMEP RLICVATVKR VVHRLLSIHF DGWDSEYDQW VDCESPDIYP VGWCELTGYQ 610 620 630 640 650 660 LQPPVAAEPA TPLKAKEATK KKKKQFGKKR KRIPPTKTRP LRQGSKKPLL EDDPQGARKI 670 680 690 700 SSEPVPGEII AVRVKEEHLD VASPDKASSP ELPVSVENIK QETDD
	Isoform 2 (B) [UniParc]. Checksum: 6098B154D7387790	FASTA	614	69,008
	10 20 30 40 50 60 MEKPRSIEET PSSEPMEEEE DDDLELFGGY DSFRSYNSSV GSESSSYLEE SSEAENEDRE 70 80 90 100 110 120 AGELPTSPLH LLSPGTPRSL DGSGSEPAVC EMCGIVGTRE AFFSKTKRFC SVSCSRSYSS 130 140 150 160 170 180 NSKKASILAR LQGKPPTKKA KVLHKAAWSA KIGAFLHSQG TGQLADGTPT GQDALVLGFD 190 200 210 220 230 240 WGKFLKDHSY KAAPVSCFKH VPLYDQWEDV MKGMKVEVLN SDAVLPSRVY WIASVIQTAG 250 260 270 280 290 300 YRVLLRYEGF ENDASHDFWC NLGTVDVHPI GWCAINSKIL VPPRTIHAKF TDWKGYLMKR 310 320 330 340 350 360 LVGSRTLPVD FHIKMVESMK YPFRQGMRLE VVDKSQVSRT RMAVVDTVIG GRLRLLYEDG 370 380 390 400 410 420 DSDDDFWCHM WSPLIHPVGW SRRVGHGIKM SERRSDMAHH PTFRKIYCDA VPYLFKKVRA 430 440 450 460 470 480 VYTEGGWFEE GMKLEAIDPL NLGNICVATV CKVLLDGYLM ICVDGGPSTD GLDWFCYHAS 490 500 510 520 530 540 SHAIFPATFC QKNDIELTPP KGYEAQTFNW ENYLEKTKSK AAPSRLFNMD CPNHGFKVGM 550 560 570 580 590 600 KLEAVDLMEP RLICVATVKR VVHRLLSIHF DGWDSEYDQW VDCESPDIYP VGWCELTGYQ 610 LQPPVAAGKL PRSL
	Isoform 3 [UniParc]. Checksum: 2AD8D020C5715608	FASTA	617	69,264
	10 20 30 40 50 60 MEKPRSIEET PSSEPMEEEE DDDLELFGGY DSFRSYNSSV GSESSSYLEE SSEAENEDRE 70 80 90 100 110 120 AGELPTSPLH LLSPGTPRSL DGSGSEPAVC EMCGIVGTRE AFFSKTKRFC SVSCSRSYSS 130 140 150 160 170 180 NSKKASILAR LQGKPPTKKA KVLHKAAWSA KIGAFLHSQG TGQLADGTPT GQDALVLGFD 190 200 210 220 230 240 WGKFLKDHSY KAAPVSCFKH VPLYDQWEDV MKGMKVEVLN SDAVLPSRVY WIASVIQTAG 250 260 270 280 290 300 YRVLLRYEGF ENDASHDFWC NLGTVDVHPI GWCAINSKIL VPPRTIHAKF TDWKGYLMKR 310 320 330 340 350 360 LVGSRTLPVD FHIKMVESMK YPFRQGMRLE VVDKSQVSRT RMAVVDTVIG GRLRLLYEDG 370 380 390 400 410 420 DSDDDFWCHM WSPLIHPVGW SRRVGHGIKM SERRSDMAHH PTFRKIYCDA VPYLFKKVRA 430 440 450 460 470 480 VYTEGGWFEE GMKLEAIDPL NLGNICVATV CKVLLDGYLM ICVDGGPSTD GLDWFCYHAS 490 500 510 520 530 540 SHAIFPATFC QKNDIELTPP KGYEAQTFNW ENYLEKTKSK AAPSRLFNMD CPNHGFKVGM 550 560 570 580 590 600 KLEAVDLMEP RLICVATVKR VVHRLLSIHF DGWDSEYDQW VDCESPDIYP VGWCELTGYQ 610 LQPPVAAGVG SRGPKRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of h-l(3)mbt-like: a new member of the human mbt family." Wismar J. FEBS Lett. 507:119-121(2001) [PubMed: 11682070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Amygdala.
[3]	"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 3). Tissue: Small intestine and Spleen.
[4]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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). Tissue: Placenta.
[7]	"A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells." Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y. Science 296:1132-1136(2002) [PubMed: 12004135] [Abstract] Cited for: IDENTIFICATION OF COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; CBX3; RING1; RNF2; MBLR; BAT8 AND YAF2.
[8]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66 AND THR-76, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-13; SER-683; SER-688 AND SER-689, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2." Guo Y., Nady N., Qi C., Allali-Hassani A., Zhu H., Pan P., Adams-Cioaba M.A., Amaya M.F., Dong A., Vedadi M., Schapira M., Read R.J., Arrowsmith C.H., Min J. Nucleic Acids Res. 37:2204-2210(2009) [PubMed: 19233876] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 170-625 IN COMPLEX WITH MONOMETHYLATED HISTONE H4 PEPTIDE, FUNCTION.
[13]	"Solution structure of the FCS zinc finger domain of the human polycomb group protein L(3)mbt-like 2." Lechtenberg B.C., Allen M.D., Rutherford T.J., Freund S.M., Bycroft M. Protein Sci. 18:657-661(2009) [PubMed: 19241375] [Abstract] Cited for: STRUCTURE BY NMR OF 82-124 IN COMPLEX WITH ZINC IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ305226 mRNA. Translation: CAC37794.1.
AJ305227 mRNA. Translation: CAC37795.1.
AL136564 mRNA. Translation: CAB66499.2.
AK074091 mRNA. Translation: BAB84917.1. Sequence problems.
AK097052 mRNA. Translation: BAC04936.1. Sequence problems.
CR456482 mRNA. Translation: CAG30368.1.
AL035658, AL035681 Genomic DNA. Translation: CAI23036.1.
AL035681, AL035658 Genomic DNA. Translation: CAI22654.1.
BC017191 mRNA. Translation: AAH17191.1.

IPI

IPI00100041.
IPI00219058.
IPI00302544.

RefSeq

NP_113676.2. NM_031488.4.

UniGene

Hs.517641.
Hs.627409.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2W0T	NMR	-	A	82-124	[»]
3CEY	X-ray	2.20	A/B	170-625	[»]
3F70	X-ray	2.10	A/B	170-625	[»]

ProteinModelPortal

Q969R5.

SMR

Q969R5. Positions 82-124, 172-609.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q969R5. 5 interactions.

MINT

MINT-1483852.

STRING

Q969R5.

PTM databases

PhosphoSite

Q969R5.

Polymorphism databases

DMDM

27734418.

Proteomic databases

PRIDE

Q969R5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216237; ENSP00000216237; ENSG00000100395.

GeneID

83746.

KEGG

hsa:83746.

UCSC

uc003azo.1. human.
uc010gyi.1. human.

Organism-specific databases

CTD

83746.

GeneCards

GC22P041601.

H-InvDB

HIX0016512.

HGNC

HGNC:18594. L3MBTL2.

HPA

HPA000815.

MIM

611865. gene.

neXtProt

NX_Q969R5.

PharmGKB

PA38356.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12325.

GeneTree

ENSGT00560000077079.

HOGENOM

HBG443880.

HOVERGEN

HBG057974.

InParanoid

Q969R5.

OMA

VATICKV.

OrthoDB

EOG4MW860.

PhylomeDB

Q969R5.

Gene expression databases

ArrayExpress

Q969R5.

Bgee

Q969R5.

CleanEx

HS_L3MBTL2.

Genevestigator

Q969R5.

GermOnline

ENSG00000100395. Homo sapiens.

Family and domain databases

InterPro

IPR004092. Mbt.
IPR012313. Znf_FCS.
[Graphical view]

Pfam

PF02820. MBT. 4 hits.
[Graphical view]

SMART

SM00561. MBT. 4 hits.
[Graphical view]

PROSITE

PS51079. MBT. 4 hits.
PS51024. ZF_FCS. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

72771.

SOURCE

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Entry information

Entry name

LMBL2_HUMAN

Accession

Primary (citable) accession number: Q969R5
Secondary accession number(s): Q8TEN1 , Q96SC4, Q9BQI2, Q9UGS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2003
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 102 of the entry and version 1 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.