Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q969R5

- LMBL2_HUMAN

UniProt

Q969R5 - LMBL2_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: IntAct
    4. 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

    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

    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

    ArrayExpressiQ969R5.
    BgeeiQ969R5.
    CleanExiHS_L3MBTL2.
    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. 21 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.
    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

    MEKPRSIEET PSSEPMEEEE DDDLELFGGY DSFRSYNSSV GSESSSYLEE    50
    SSEAENEDRE AGELPTSPLH LLSPGTPRSL DGSGSEPAVC EMCGIVGTRE 100
    AFFSKTKRFC SVSCSRSYSS NSKKASILAR LQGKPPTKKA KVLHKAAWSA 150
    KIGAFLHSQG TGQLADGTPT GQDALVLGFD WGKFLKDHSY KAAPVSCFKH 200
    VPLYDQWEDV MKGMKVEVLN SDAVLPSRVY WIASVIQTAG YRVLLRYEGF 250
    ENDASHDFWC NLGTVDVHPI GWCAINSKIL VPPRTIHAKF TDWKGYLMKR 300
    LVGSRTLPVD FHIKMVESMK YPFRQGMRLE VVDKSQVSRT RMAVVDTVIG 350
    GRLRLLYEDG DSDDDFWCHM WSPLIHPVGW SRRVGHGIKM SERRSDMAHH 400
    PTFRKIYCDA VPYLFKKVRA VYTEGGWFEE GMKLEAIDPL NLGNICVATV 450
    CKVLLDGYLM ICVDGGPSTD GLDWFCYHAS SHAIFPATFC QKNDIELTPP 500
    KGYEAQTFNW ENYLEKTKSK AAPSRLFNMD CPNHGFKVGM KLEAVDLMEP 550
    RLICVATVKR VVHRLLSIHF DGWDSEYDQW VDCESPDIYP VGWCELTGYQ 600
    LQPPVAAEPA TPLKAKEATK KKKKQFGKKR KRIPPTKTRP LRQGSKKPLL 650
    EDDPQGARKI SSEPVPGEII AVRVKEEHLD VASPDKASSP ELPVSVENIK 700
    QETDD 705
    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. 21 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.
    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

    ArrayExpressi Q969R5.
    Bgeei Q969R5.
    CleanExi HS_L3MBTL2.
    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

    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 1, 2014
    This is version 129 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