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Q8TEK3

- DOT1L_HUMAN

UniProt

Q8TEK3 - DOT1L_HUMAN

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Protein
Histone-lysine N-methyltransferase, H3 lysine-79 specific
Gene
DOT1L, KIAA1814, KMT4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publication

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi312 – 3121Y → A: Loss of activity. 1 Publication
Mutagenesisi312 – 3121Y → F: No effect. 1 Publication

Organism-specific databases

PharmGKBiPA134993717.

PTM / Processingi

Molecule processing

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

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.

Miscellaneous databases

EvolutionaryTraceiQ8TEK3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 330315DOT1
Add
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 DNA
Add
BLAST

Sequence similaritiesi

Contains 1 DOT1 domain.

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.

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.
VSP_002228
Alternative sequencei1538 – 1739202Missing in isoform 1.
VSP_002229Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101G → E in BAB84946. 1 Publication
Sequence conflicti454 – 46714RSPHS…LPPSV → TLRTPSGSPRRTKL1 Publication
Add
BLAST
Sequence conflicti464 – 4641P → L in BAB84946. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 126 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

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