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Q969R5

- LMBL2_HUMAN

UniProt

Q969R5 - LMBL2_HUMAN

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Protein

Lethal(3)malignant brain tumor-like protein 2

Gene

L3MBTL2

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

Functioni

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'.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri81 – 11636FCS-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. histone binding Source: UniProtKB
  2. methylated histone binding Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:L3MBTL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:18594. L3MBTL2.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38356.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 705705Lethal(3)malignant brain tumor-like protein 2PRO_0000084448Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei338 – 3381Phosphoserine1 Publication
Modified residuei683 – 6831Phosphoserine1 Publication
Modified residuei688 – 6881Phosphoserine1 Publication
Modified residuei689 – 6891Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ969R5.
PaxDbiQ969R5.
PRIDEiQ969R5.

PTM databases

PhosphoSiteiQ969R5.

Expressioni

Gene expression databases

BgeeiQ969R5.
CleanExiHS_L3MBTL2.
ExpressionAtlasiQ969R5. baseline and differential.
GenevestigatoriQ969R5.

Organism-specific databases

HPAiHPA000815.

Interactioni

Subunit structurei

Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, BAT8 and YAF2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC3O153796EBI-739909,EBI-607682

Protein-protein interaction databases

BioGridi123753. 25 interactions.
DIPiDIP-56748N.
IntActiQ969R5. 6 interactions.
MINTiMINT-1483852.
STRINGi9606.ENSP00000216237.

Structurei

Secondary structure

1
705
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi87 – 893
Turni91 – 933
Beta strandi96 – 983
Turni99 – 1013
Turni104 – 1063
Beta strandi107 – 1115
Helixi112 – 1209
Helixi181 – 1888
Helixi195 – 1973
Helixi204 – 2096
Beta strandi215 – 2195
Beta strandi230 – 23910
Beta strandi242 – 2476
Beta strandi258 – 2614
Helixi272 – 2754
Turni284 – 2863
Helixi287 – 2893
Helixi293 – 3019
Helixi311 – 3188
Beta strandi328 – 3325
Beta strandi340 – 34910
Beta strandi352 – 3576
Beta strandi366 – 3694
Beta strandi375 – 3773
Helixi380 – 3845
Helixi412 – 4143
Beta strandi420 – 4223
Beta strandi433 – 4386
Beta strandi441 – 45313
Helixi455 – 4573
Beta strandi458 – 4636
Beta strandi475 – 4784
Beta strandi482 – 4865
Helixi489 – 4924
Beta strandi505 – 5073
Helixi510 – 5178
Helixi524 – 5263
Beta strandi541 – 5455
Beta strandi553 – 56210
Beta strandi565 – 5706
Helixi575 – 5773
Beta strandi579 – 5824
Helixi593 – 5975
Beta strandi604 – 6074

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W0TNMR-A82-124[»]
3CEYX-ray2.20A/B170-625[»]
3F70X-ray2.10A/B170-625[»]
ProteinModelPortaliQ969R5.
SMRiQ969R5. Positions 82-124, 143-626.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ969R5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati179 – 283105MBT 1Add
BLAST
Repeati291 – 391101MBT 2Add
BLAST
Repeati397 – 500104MBT 3Add
BLAST
Repeati508 – 60497MBT 4Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 204Poly-Glu
Compositional biasi620 – 6245Poly-Lys

Sequence similaritiesi

Contains 1 FCS-type zinc finger.PROSITE-ProRule annotation
Contains 4 MBT repeats.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri81 – 11636FCS-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG271713.
GeneTreeiENSGT00760000119024.
HOGENOMiHOG000231220.
HOVERGENiHBG057974.
InParanoidiQ969R5.
OMAiDGWDNEY.
OrthoDBiEOG7M98G1.
PhylomeDBiQ969R5.
TreeFamiTF316498.

Family and domain databases

InterProiIPR004092. Mbt.
IPR012313. Znf_FCS.
[Graphical view]
PfamiPF02820. MBT. 4 hits.
[Graphical view]
SMARTiSM00561. MBT. 4 hits.
[Graphical view]
PROSITEiPS51079. MBT. 4 hits.
PS51024. ZF_FCS. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q969R5-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MEKPRSIEET PSSEPMEEEE DDDLELFGGY DSFRSYNSSV GSESSSYLEE
60 70 80 90 100
SSEAENEDRE AGELPTSPLH LLSPGTPRSL DGSGSEPAVC EMCGIVGTRE
110 120 130 140 150
AFFSKTKRFC SVSCSRSYSS NSKKASILAR LQGKPPTKKA KVLHKAAWSA
160 170 180 190 200
KIGAFLHSQG TGQLADGTPT GQDALVLGFD WGKFLKDHSY KAAPVSCFKH
210 220 230 240 250
VPLYDQWEDV MKGMKVEVLN SDAVLPSRVY WIASVIQTAG YRVLLRYEGF
260 270 280 290 300
ENDASHDFWC NLGTVDVHPI GWCAINSKIL VPPRTIHAKF TDWKGYLMKR
310 320 330 340 350
LVGSRTLPVD FHIKMVESMK YPFRQGMRLE VVDKSQVSRT RMAVVDTVIG
360 370 380 390 400
GRLRLLYEDG DSDDDFWCHM WSPLIHPVGW SRRVGHGIKM SERRSDMAHH
410 420 430 440 450
PTFRKIYCDA VPYLFKKVRA VYTEGGWFEE GMKLEAIDPL NLGNICVATV
460 470 480 490 500
CKVLLDGYLM ICVDGGPSTD GLDWFCYHAS SHAIFPATFC QKNDIELTPP
510 520 530 540 550
KGYEAQTFNW ENYLEKTKSK AAPSRLFNMD CPNHGFKVGM KLEAVDLMEP
560 570 580 590 600
RLICVATVKR VVHRLLSIHF DGWDSEYDQW VDCESPDIYP VGWCELTGYQ
610 620 630 640 650
LQPPVAAEPA TPLKAKEATK KKKKQFGKKR KRIPPTKTRP LRQGSKKPLL
660 670 680 690 700
EDDPQGARKI SSEPVPGEII AVRVKEEHLD VASPDKASSP ELPVSVENIK

QETDD
Length:705
Mass (Da):79,110
Last modified:December 1, 2001 - v1
Checksum:i8FC86A440982FFA7
GO
Isoform 2 (identifier: Q969R5-2) [UniParc]FASTAAdd to Basket

Also known as: B

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

Show »
Length:614
Mass (Da):69,008
Checksum:i6098B154D7387790
GO
Isoform 3 (identifier: Q969R5-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:617
Mass (Da):69,264
Checksum:i2AD8D020C5715608
GO

Sequence cautioni

The sequence BAB84917.1 differs from that shown. Reason: Intron retention.
The sequence BAC04936.1 differs from that shown. Reason: Intron retention.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71I → V.
Corresponds to variant rs3804097 [ dbSNP | Ensembl ].
VAR_033998
Natural varianti300 – 3001R → W.
Corresponds to variant rs2277846 [ dbSNP | Ensembl ].
VAR_015093
Natural varianti337 – 3371V → A.
Corresponds to variant rs34289721 [ dbSNP | Ensembl ].
VAR_061675

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei608 – 61710EPATPLKAKE → GVGSRGPKRL in isoform 3. 1 PublicationVSP_003906
Alternative sequencei608 – 6147EPATPLK → GKLPRSL in isoform 2. 1 PublicationVSP_003904
Alternative sequencei615 – 70591Missing in isoform 2. 1 PublicationVSP_003905Add
BLAST
Alternative sequencei618 – 70588Missing in isoform 3. 1 PublicationVSP_003907Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14011.1. [Q969R5-1]
RefSeqiNP_113676.2. NM_031488.4. [Q969R5-1]
UniGeneiHs.517641.

Genome annotation databases

EnsembliENST00000216237; ENSP00000216237; ENSG00000100395. [Q969R5-1]
ENST00000452106; ENSP00000414423; ENSG00000100395. [Q969R5-2]
GeneIDi83746.
KEGGihsa:83746.
UCSCiuc003azo.3. human. [Q969R5-1]
uc010gyi.1. human. [Q969R5-3]

Polymorphism databases

DMDMi27734418.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14011.1. [Q969R5-1 ]
RefSeqi NP_113676.2. NM_031488.4. [Q969R5-1 ]
UniGenei Hs.517641.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q969R5.
SMRi Q969R5. Positions 82-124, 143-626.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123753. 25 interactions.
DIPi DIP-56748N.
IntActi Q969R5. 6 interactions.
MINTi MINT-1483852.
STRINGi 9606.ENSP00000216237.

PTM databases

PhosphoSitei Q969R5.

Polymorphism databases

DMDMi 27734418.

Proteomic databases

MaxQBi Q969R5.
PaxDbi Q969R5.
PRIDEi Q969R5.

Protocols and materials databases

DNASUi 83746.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216237 ; ENSP00000216237 ; ENSG00000100395 . [Q969R5-1 ]
ENST00000452106 ; ENSP00000414423 ; ENSG00000100395 . [Q969R5-2 ]
GeneIDi 83746.
KEGGi hsa:83746.
UCSCi uc003azo.3. human. [Q969R5-1 ]
uc010gyi.1. human. [Q969R5-3 ]

Organism-specific databases

CTDi 83746.
GeneCardsi GC22P041601.
HGNCi HGNC:18594. L3MBTL2.
HPAi HPA000815.
MIMi 611865. gene.
neXtProti NX_Q969R5.
PharmGKBi PA38356.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271713.
GeneTreei ENSGT00760000119024.
HOGENOMi HOG000231220.
HOVERGENi HBG057974.
InParanoidi Q969R5.
OMAi DGWDNEY.
OrthoDBi EOG7M98G1.
PhylomeDBi Q969R5.
TreeFami TF316498.

Miscellaneous databases

ChiTaRSi L3MBTL2. human.
EvolutionaryTracei Q969R5.
GeneWikii L3MBTL2.
GenomeRNAii 83746.
NextBioi 72771.
PROi Q969R5.
SOURCEi Search...

Gene expression databases

Bgeei Q969R5.
CleanExi HS_L3MBTL2.
ExpressionAtlasi Q969R5. baseline and differential.
Genevestigatori Q969R5.

Family and domain databases

InterProi IPR004092. Mbt.
IPR012313. Znf_FCS.
[Graphical view ]
Pfami PF02820. MBT. 4 hits.
[Graphical view ]
SMARTi SM00561. MBT. 4 hits.
[Graphical view ]
PROSITEi PS51079. MBT. 4 hits.
PS51024. ZF_FCS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Small intestine and Spleen.
  4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; CBX3; RING1; RNF2; MBLR; BAT8 AND YAF2.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-683; SER-688 AND SER-689, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. 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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 82-124 IN COMPLEX WITH ZINC IONS.

Entry informationi

Entry nameiLMBL2_HUMAN
AccessioniPrimary (citable) accession number: Q969R5
Secondary accession number(s): Q8TEN1
, Q96SC4, Q9BQI2, Q9UGS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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

External Data

Dasty 3