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Q8TEK3

- DOT1L_HUMAN

UniProt

Q8TEK3 - DOT1L_HUMAN

Protein

Histone-lysine N-methyltransferase, H3 lysine-79 specific

Gene

DOT1L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (15 Nov 2002)
      Previous versions | rss
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    Functioni

    Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA.

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 PublicationPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei186 – 1861S-adenosyl-L-methionine

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. histone-lysine N-methyltransferase activity Source: UniProtKB
    3. protein binding Source: IntAct
    4. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. histone lysine methylation Source: GOC
    2. regulation of JAK-STAT cascade Source: UniProtKB
    3. regulation of transcription regulatory region DNA binding Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Ligandi

    DNA-binding, S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC:2.1.1.43)
    Alternative name(s):
    DOT1-like protein
    Histone H3-K79 methyltransferase
    Short name:
    H3-K79-HMTase
    Lysine N-methyltransferase 4
    Gene namesi
    Name:DOT1L
    Synonyms:KIAA1814, KMT4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:24948. DOT1L.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi163 – 1653GSG → RCR: Abolishes methyltransferase activity. 1 Publication
    Mutagenesisi241 – 2411N → A or D: Loss of activity. 2 Publications
    Mutagenesisi312 – 3121Y → A: Loss of activity. 2 Publications
    Mutagenesisi312 – 3121Y → F: No effect. 2 Publications

    Organism-specific databases

    PharmGKBiPA134993717.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17391739Histone-lysine N-methyltransferase, H3 lysine-79 specificPRO_0000186089Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei374 – 3741Phosphoserine4 Publications
    Modified residuei471 – 4711Phosphoserine1 Publication
    Modified residuei480 – 4801Phosphothreonine1 Publication
    Modified residuei775 – 7751Phosphoserine2 Publications
    Modified residuei834 – 8341Phosphoserine1 Publication
    Modified residuei900 – 9001Phosphothreonine1 Publication
    Modified residuei902 – 9021Phosphoserine3 Publications
    Modified residuei1001 – 10011Phosphoserine4 Publications
    Modified residuei1009 – 10091Phosphoserine1 Publication
    Modified residuei1035 – 10351Phosphoserine1 Publication
    Modified residuei1213 – 12131Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8TEK3.
    PaxDbiQ8TEK3.
    PRIDEiQ8TEK3.

    PTM databases

    PhosphoSiteiQ8TEK3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8TEK3.
    BgeeiQ8TEK3.
    CleanExiHS_DOT1L.
    GenevestigatoriQ8TEK3.

    Interactioni

    Subunit structurei

    Interacts with MLLT10.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MLLT1Q031116EBI-2619253,EBI-1384215
    MLLT3P425683EBI-2619253,EBI-716132

    Protein-protein interaction databases

    BioGridi124082. 27 interactions.
    DIPiDIP-56410N.
    IntActiQ8TEK3. 8 interactions.
    MINTiMINT-6611327.
    STRINGi9606.ENSP00000381657.

    Structurei

    Secondary structure

    1
    1739
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 94
    Beta strandi18 – 236
    Beta strandi26 – 283
    Helixi33 – 4715
    Helixi49 – 546
    Helixi57 – 626
    Helixi68 – 9023
    Beta strandi91 – 933
    Beta strandi98 – 1003
    Helixi104 – 11815
    Helixi122 – 1243
    Helixi126 – 1283
    Beta strandi129 – 1313
    Helixi133 – 1386
    Helixi140 – 15112
    Beta strandi158 – 1636
    Helixi168 – 1769
    Beta strandi180 – 1867
    Helixi189 – 20921
    Beta strandi215 – 2206
    Helixi226 – 2338
    Beta strandi236 – 2405
    Turni243 – 2453
    Helixi247 – 25711
    Beta strandi265 – 2706
    Beta strandi281 – 2833
    Helixi287 – 2893
    Beta strandi290 – 2956
    Beta strandi307 – 3093
    Beta strandi313 – 3175
    Helixi320 – 33011
    Helixi332 – 34211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NW3X-ray2.50A1-416[»]
    3QOWX-ray2.10A1-416[»]
    3QOXX-ray2.30A1-416[»]
    3SR4X-ray2.50A1-351[»]
    3SX0X-ray2.28A1-420[»]
    3UWPX-ray2.05A1-420[»]
    4EK9X-ray2.50A1-416[»]
    4EKGX-ray2.80A1-416[»]
    4EKIX-ray2.85A1-416[»]
    4EQZX-ray2.15A1-420[»]
    4ER0X-ray2.50A1-420[»]
    4ER3X-ray2.40A1-351[»]
    4ER5X-ray2.57A1-412[»]
    4ER6X-ray2.30A1-412[»]
    4ER7X-ray2.20A1-420[»]
    4HRAX-ray3.15A1-416[»]
    ProteinModelPortaliQ8TEK3.
    SMRiQ8TEK3. Positions 4-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8TEK3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 330315DOT1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni136 – 1394S-adenosyl-L-methionine binding
    Regioni159 – 16810S-adenosyl-L-methionine binding
    Regioni222 – 2232S-adenosyl-L-methionine binding
    Regioni391 – 41626Required for interaction with nucleosomes and DNAAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.PROSITE-ProRule annotation
    Contains 1 DOT1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG294902.
    HOGENOMiHOG000143530.
    HOVERGENiHBG051393.
    InParanoidiQ8TEK3.
    KOiK11427.
    OMAiWIESEAF.
    OrthoDBiEOG7W6WJV.
    PhylomeDBiQ8TEK3.
    TreeFamiTF106393.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR017956. AT_hook_DNA-bd_motif.
    IPR013110. DOT1.
    IPR025789. Histone_H3-K79_MeTrfase.
    IPR021169. Histone_H3-K79_MeTrfase_met.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF08123. DOT1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037123. Histone_H3-K79_MeTrfase_met. 1 hit.
    SMARTiSM00384. AT_hook. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51569. DOT1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q8TEK3-1) [UniParc]FASTAAdd to Basket

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

    « Hide

    MGEKLELRLK SPVGAEPAVY PWPLPVYDKH HDAAHEIIET IRWVCEEIPD     50
    LKLAMENYVL IDYDTKSFES MQRLCDKYNR AIDSIHQLWK GTTQPMKLNT 100
    RPSTGLLRHI LQQVYNHSVT DPEKLNNYEP FSPEVYGETS FDLVAQMIDE 150
    IKMTDDDLFV DLGSGVGQVV LQVAAATNCK HHYGVEKADI PAKYAETMDR 200
    EFRKWMKWYG KKHAEYTLER GDFLSEEWRE RIANTSVIFV NNFAFGPEVD 250
    HQLKERFANM KEGGRIVSSK PFAPLNFRIN SRNLSDIGTI MRVVELSPLK 300
    GSVSWTGKPV SYYLHTIDRT ILENYFSSLK NPKLREEQEA ARRRQQRESK 350
    SNAATPTKGP EGKVAGPADA PMDSGAEEEK AGAATVKKPS PSKARKKKLN 400
    KKGRKMAGRK RGRPKKMNTA NPERKPKKNQ TALDALHAQT VSQTAASSPQ 450
    DAYRSPHSPF YQLPPSVQRH SPNPLLVAPT PPALQKLLES FKIQYLQFLA 500
    YTKTPQYKAS LQELLGQEKE KNAQLLGAAQ QLLSHCQAQK EEIRRLFQQK 550
    LDELGVKALT YNDLIQAQKE ISAHNQQLRE QSEQLEQDNR ALRGQSLQLL 600
    KARCEELQLD WATLSLEKLL KEKQALKSQI SEKQRHCLEL QISIVELEKS 650
    QRQQELLQLK SCVPPDDALS LHLRGKGALG RELEPDASRL HLELDCTKFS 700
    LPHLSSMSPE LSMNGQAAGY ELCGVLSRPS SKQNTPQYLA SPLDQEVVPC 750
    TPSHVGRPRL EKLSGLAAPD YTRLSPAKIV LRRHLSQDHT VPGRPAASEL 800
    HSRAEHTKEN GLPYQSPSVP GSMKLSPQDP RPLSPGALQL AGEKSSEKGL 850
    RERAYGSSGE LITSLPISIP LSTVQPNKLP VSIPLASVVL PSRAERARST 900
    PSPVLQPRDP SSTLEKQIGA NAHGAGSRSL ALAPAGFSYA GSVAISGALA 950
    GSPASLTPGA EPATLDESSS SGSLFATVGS RSSTPQHPLL LAQPRNSLPA 1000
    SPAHQLSSSP RLGGAAQGPL PEASKGDLPS DSGFSDPESE AKRRIVFTIT 1050
    TGAGSAKQSP SSKHSPLTAS ARGDCVPSHG QDSRRRGRRK RASAGTPSLS 1100
    AGVSPKRRAL PSVAGLFTQP SGSPLNLNSM VSNINQPLEI TAISSPETSL 1150
    KSSPVPYQDH DQPPVLKKER PLSQTNGAHY SPLTSDEEPG SEDEPSSARI 1200
    ERKIATISLE SKSPPKTLEN GGGLAGRKPA PAGEPVNSSK WKSTFSPISD 1250
    IGLAKSADSP LQASSALSQN SLFTFRPALE EPSADAKLAA HPRKGFPGSL 1300
    SGADGLSPGT NPANGCTFGG GLAADLSLHS FSDGASLPHK GPEAAGLSSP 1350
    LSFPSQRGKE GSDANPFLSK RQLDGLAGLK GEGSRGKEAG EGGLPLCGPT 1400
    DKTPLLSGKA AKARDREVDL KNGHNLFISA AAVPPGSLLS GPGLAPAASS 1450
    AGGAASSAQT HRSFLGPFPP GPQFALGPMS LQANLGSVAG SSVLQSLFSS 1500
    VPAAAGLVHV SSAATRLTNS HAMGSFSGVA GGTVGGVVFN HAVPSASAHP 1550
    FGARVGRGAA CGSATLGPSP LQAAASASAS SFQAPASVET RPPPPPPPPP 1600
    PPLPPPAHLG RSPAGPPVLH APPPPNAALP PPPTLLASNP EPALLQSLAS 1650
    LPPNQAFLPP TSAASLPPAN ASLSIKLTSL PHKGARPSFT VHHQPLPRLA 1700
    LAQAAPGIPQ ASATGPSAVW VSLGMPPPYA AHLSGVKPR 1739
    Length:1,739
    Mass (Da):184,853
    Last modified:November 15, 2002 - v2
    Checksum:iEBA575CE3C090CAC
    GO
    Isoform 1 (identifier: Q8TEK3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1537-1537: V → N
         1538-1739: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,537
    Mass (Da):164,856
    Checksum:i9CEA12850DC4ACB1
    GO

    Sequence cautioni

    The sequence AAC08316.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti210 – 2101G → E in BAB84946. (PubMed:12693554)Curated
    Sequence conflicti454 – 46714RSPHS…LPPSV → TLRTPSGSPRRTKL(PubMed:11347906)CuratedAdd
    BLAST
    Sequence conflicti464 – 4641P → L in BAB84946. (PubMed:12693554)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti726 – 7261L → M.
    Corresponds to variant rs880525 [ dbSNP | Ensembl ].
    VAR_014287
    Natural varianti1386 – 13861G → S.
    Corresponds to variant rs3815308 [ dbSNP | Ensembl ].
    VAR_014288
    Natural varianti1418 – 14181V → L.
    Corresponds to variant rs2302061 [ dbSNP | Ensembl ].
    VAR_014289

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1537 – 15371V → N in isoform 1. 1 PublicationVSP_002228
    Alternative sequencei1538 – 1739202Missing in isoform 1. 1 PublicationVSP_002229Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF509504 mRNA. Translation: AAM88322.1.
    AC004490 Genomic DNA. Translation: AAC08316.1. Sequence problems.
    AB058717 mRNA. Translation: BAB47443.1.
    AK074120 mRNA. Translation: BAB84946.1.
    CCDSiCCDS42460.1. [Q8TEK3-2]
    RefSeqiNP_115871.1. NM_032482.2. [Q8TEK3-2]
    UniGeneiHs.713641.

    Genome annotation databases

    EnsembliENST00000398665; ENSP00000381657; ENSG00000104885. [Q8TEK3-2]
    GeneIDi84444.
    KEGGihsa:84444.
    UCSCiuc002lvb.4. human. [Q8TEK3-2]
    uc002lvc.1. human. [Q8TEK3-1]

    Polymorphism databases

    DMDMi25090171.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF509504 mRNA. Translation: AAM88322.1 .
    AC004490 Genomic DNA. Translation: AAC08316.1 . Sequence problems.
    AB058717 mRNA. Translation: BAB47443.1 .
    AK074120 mRNA. Translation: BAB84946.1 .
    CCDSi CCDS42460.1. [Q8TEK3-2 ]
    RefSeqi NP_115871.1. NM_032482.2. [Q8TEK3-2 ]
    UniGenei Hs.713641.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NW3 X-ray 2.50 A 1-416 [» ]
    3QOW X-ray 2.10 A 1-416 [» ]
    3QOX X-ray 2.30 A 1-416 [» ]
    3SR4 X-ray 2.50 A 1-351 [» ]
    3SX0 X-ray 2.28 A 1-420 [» ]
    3UWP X-ray 2.05 A 1-420 [» ]
    4EK9 X-ray 2.50 A 1-416 [» ]
    4EKG X-ray 2.80 A 1-416 [» ]
    4EKI X-ray 2.85 A 1-416 [» ]
    4EQZ X-ray 2.15 A 1-420 [» ]
    4ER0 X-ray 2.50 A 1-420 [» ]
    4ER3 X-ray 2.40 A 1-351 [» ]
    4ER5 X-ray 2.57 A 1-412 [» ]
    4ER6 X-ray 2.30 A 1-412 [» ]
    4ER7 X-ray 2.20 A 1-420 [» ]
    4HRA X-ray 3.15 A 1-416 [» ]
    ProteinModelPortali Q8TEK3.
    SMRi Q8TEK3. Positions 4-344.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124082. 27 interactions.
    DIPi DIP-56410N.
    IntActi Q8TEK3. 8 interactions.
    MINTi MINT-6611327.
    STRINGi 9606.ENSP00000381657.

    Chemistry

    ChEMBLi CHEMBL1795117.
    GuidetoPHARMACOLOGYi 2650.

    PTM databases

    PhosphoSitei Q8TEK3.

    Polymorphism databases

    DMDMi 25090171.

    Proteomic databases

    MaxQBi Q8TEK3.
    PaxDbi Q8TEK3.
    PRIDEi Q8TEK3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398665 ; ENSP00000381657 ; ENSG00000104885 . [Q8TEK3-2 ]
    GeneIDi 84444.
    KEGGi hsa:84444.
    UCSCi uc002lvb.4. human. [Q8TEK3-2 ]
    uc002lvc.1. human. [Q8TEK3-1 ]

    Organism-specific databases

    CTDi 84444.
    GeneCardsi GC19P002115.
    HGNCi HGNC:24948. DOT1L.
    MIMi 607375. gene.
    neXtProti NX_Q8TEK3.
    PharmGKBi PA134993717.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG294902.
    HOGENOMi HOG000143530.
    HOVERGENi HBG051393.
    InParanoidi Q8TEK3.
    KOi K11427.
    OMAi WIESEAF.
    OrthoDBi EOG7W6WJV.
    PhylomeDBi Q8TEK3.
    TreeFami TF106393.

    Miscellaneous databases

    ChiTaRSi DOT1L. human.
    EvolutionaryTracei Q8TEK3.
    GeneWikii DOT1L.
    GenomeRNAii 84444.
    NextBioi 74205.
    PROi Q8TEK3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TEK3.
    Bgeei Q8TEK3.
    CleanExi HS_DOT1L.
    Genevestigatori Q8TEK3.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR017956. AT_hook_DNA-bd_motif.
    IPR013110. DOT1.
    IPR025789. Histone_H3-K79_MeTrfase.
    IPR021169. Histone_H3-K79_MeTrfase_met.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF08123. DOT1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037123. Histone_H3-K79_MeTrfase_met. 1 hit.
    SMARTi SM00384. AT_hook. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51569. DOT1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain."
      Feng Q., Wang H., Ng H.H., Erdjument-Bromage H., Tempst P., Struhl K., Zhang Y.
      Curr. Biol. 12:1052-1058(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, MUTAGENESIS OF 163-GLY--GLY-165.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
      DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-1739 (ISOFORM 2).
      Tissue: Brain.
    4. "Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
      Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
      DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Spleen.
    5. "hDOT1L links histone methylation to leukemogenesis."
      Okada Y., Feng Q., Lin Y., Jiang Q., Li Y., Coffield V.M., Su L., Xu G., Zhang Y.
      Cell 121:167-178(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLLT10, SUBCELLULAR LOCATION.
    6. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-775; SER-1001 AND SER-1009, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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].
    9. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; THR-900; SER-902 AND SER-1001, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-471; THR-480; SER-775; SER-834; SER-902; SER-1001; SER-1035 AND SER-1213, 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-374 AND SER-902, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase."
      Min J., Feng Q., Li Z., Zhang Y., Xu R.-M.
      Cell 112:711-723(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-416 IN COMPLEX WITH S-ADENOSINE-L-METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF ASN-241 AND TYR-312, NUCLEOSOME BINDING, INTERACTION WITH DNA.

    Entry informationi

    Entry nameiDOT1L_HUMAN
    AccessioniPrimary (citable) accession number: Q8TEK3
    Secondary accession number(s): O60379, Q96JL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: November 15, 2002
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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