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Protein

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

Gene

DOT1L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 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. 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 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

BgeeiQ8TEK3.
CleanExiHS_DOT1L.
ExpressionAtlasiQ8TEK3. baseline and differential.
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 – 94Combined sources
Beta strandi18 – 236Combined sources
Beta strandi26 – 283Combined sources
Helixi33 – 4715Combined sources
Helixi49 – 546Combined sources
Helixi57 – 626Combined sources
Helixi68 – 9023Combined sources
Beta strandi91 – 933Combined sources
Beta strandi98 – 1003Combined sources
Helixi104 – 11815Combined sources
Helixi122 – 1243Combined sources
Helixi126 – 1283Combined sources
Beta strandi129 – 1313Combined sources
Helixi133 – 1386Combined sources
Helixi140 – 15112Combined sources
Beta strandi158 – 1636Combined sources
Helixi168 – 1769Combined sources
Beta strandi180 – 1867Combined sources
Helixi189 – 20921Combined sources
Beta strandi215 – 2206Combined sources
Helixi226 – 2338Combined sources
Beta strandi236 – 2405Combined sources
Turni243 – 2453Combined sources
Helixi247 – 25711Combined sources
Beta strandi265 – 2706Combined sources
Beta strandi281 – 2833Combined sources
Helixi287 – 2893Combined sources
Beta strandi290 – 2956Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi313 – 3175Combined sources
Helixi320 – 33011Combined sources
Helixi332 – 34211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4WVLX-ray2.41A1-347[»]
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.
GeneTreeiENSGT00390000013515.
HOGENOMiHOG000143530.
HOVERGENiHBG051393.
InParanoidiQ8TEK3.
KOiK11427.
OMAiNGLPYQS.
OrthoDBiEOG7W6WJV.
PhylomeDBiQ8TEK3.
TreeFamiTF106393.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR025789. DOT1_dom.
IPR013110. DOT1_dom_Pfam.
IPR021169. DOT1L/grappa.
IPR029063. SAM-dependent_MTases.
[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

        10         20         30         40         50
MGEKLELRLK SPVGAEPAVY PWPLPVYDKH HDAAHEIIET IRWVCEEIPD
60 70 80 90 100
LKLAMENYVL IDYDTKSFES MQRLCDKYNR AIDSIHQLWK GTTQPMKLNT
110 120 130 140 150
RPSTGLLRHI LQQVYNHSVT DPEKLNNYEP FSPEVYGETS FDLVAQMIDE
160 170 180 190 200
IKMTDDDLFV DLGSGVGQVV LQVAAATNCK HHYGVEKADI PAKYAETMDR
210 220 230 240 250
EFRKWMKWYG KKHAEYTLER GDFLSEEWRE RIANTSVIFV NNFAFGPEVD
260 270 280 290 300
HQLKERFANM KEGGRIVSSK PFAPLNFRIN SRNLSDIGTI MRVVELSPLK
310 320 330 340 350
GSVSWTGKPV SYYLHTIDRT ILENYFSSLK NPKLREEQEA ARRRQQRESK
360 370 380 390 400
SNAATPTKGP EGKVAGPADA PMDSGAEEEK AGAATVKKPS PSKARKKKLN
410 420 430 440 450
KKGRKMAGRK RGRPKKMNTA NPERKPKKNQ TALDALHAQT VSQTAASSPQ
460 470 480 490 500
DAYRSPHSPF YQLPPSVQRH SPNPLLVAPT PPALQKLLES FKIQYLQFLA
510 520 530 540 550
YTKTPQYKAS LQELLGQEKE KNAQLLGAAQ QLLSHCQAQK EEIRRLFQQK
560 570 580 590 600
LDELGVKALT YNDLIQAQKE ISAHNQQLRE QSEQLEQDNR ALRGQSLQLL
610 620 630 640 650
KARCEELQLD WATLSLEKLL KEKQALKSQI SEKQRHCLEL QISIVELEKS
660 670 680 690 700
QRQQELLQLK SCVPPDDALS LHLRGKGALG RELEPDASRL HLELDCTKFS
710 720 730 740 750
LPHLSSMSPE LSMNGQAAGY ELCGVLSRPS SKQNTPQYLA SPLDQEVVPC
760 770 780 790 800
TPSHVGRPRL EKLSGLAAPD YTRLSPAKIV LRRHLSQDHT VPGRPAASEL
810 820 830 840 850
HSRAEHTKEN GLPYQSPSVP GSMKLSPQDP RPLSPGALQL AGEKSSEKGL
860 870 880 890 900
RERAYGSSGE LITSLPISIP LSTVQPNKLP VSIPLASVVL PSRAERARST
910 920 930 940 950
PSPVLQPRDP SSTLEKQIGA NAHGAGSRSL ALAPAGFSYA GSVAISGALA
960 970 980 990 1000
GSPASLTPGA EPATLDESSS SGSLFATVGS RSSTPQHPLL LAQPRNSLPA
1010 1020 1030 1040 1050
SPAHQLSSSP RLGGAAQGPL PEASKGDLPS DSGFSDPESE AKRRIVFTIT
1060 1070 1080 1090 1100
TGAGSAKQSP SSKHSPLTAS ARGDCVPSHG QDSRRRGRRK RASAGTPSLS
1110 1120 1130 1140 1150
AGVSPKRRAL PSVAGLFTQP SGSPLNLNSM VSNINQPLEI TAISSPETSL
1160 1170 1180 1190 1200
KSSPVPYQDH DQPPVLKKER PLSQTNGAHY SPLTSDEEPG SEDEPSSARI
1210 1220 1230 1240 1250
ERKIATISLE SKSPPKTLEN GGGLAGRKPA PAGEPVNSSK WKSTFSPISD
1260 1270 1280 1290 1300
IGLAKSADSP LQASSALSQN SLFTFRPALE EPSADAKLAA HPRKGFPGSL
1310 1320 1330 1340 1350
SGADGLSPGT NPANGCTFGG GLAADLSLHS FSDGASLPHK GPEAAGLSSP
1360 1370 1380 1390 1400
LSFPSQRGKE GSDANPFLSK RQLDGLAGLK GEGSRGKEAG EGGLPLCGPT
1410 1420 1430 1440 1450
DKTPLLSGKA AKARDREVDL KNGHNLFISA AAVPPGSLLS GPGLAPAASS
1460 1470 1480 1490 1500
AGGAASSAQT HRSFLGPFPP GPQFALGPMS LQANLGSVAG SSVLQSLFSS
1510 1520 1530 1540 1550
VPAAAGLVHV SSAATRLTNS HAMGSFSGVA GGTVGGVVFN HAVPSASAHP
1560 1570 1580 1590 1600
FGARVGRGAA CGSATLGPSP LQAAASASAS SFQAPASVET RPPPPPPPPP
1610 1620 1630 1640 1650
PPLPPPAHLG RSPAGPPVLH APPPPNAALP PPPTLLASNP EPALLQSLAS
1660 1670 1680 1690 1700
LPPNQAFLPP TSAASLPPAN ASLSIKLTSL PHKGARPSFT VHHQPLPRLA
1710 1720 1730
LAQAAPGIPQ ASATGPSAVW VSLGMPPPYA AHLSGVKPR
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4WVLX-ray2.41A1-347[»]
ProteinModelPortaliQ8TEK3.
SMRiQ8TEK3. Positions 4-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiQ8TEK3.
ChEMBLiCHEMBL1795117.
GuidetoPHARMACOLOGYi2650.

PTM databases

PhosphoSiteiQ8TEK3.

Polymorphism databases

DMDMi25090171.

Proteomic databases

MaxQBiQ8TEK3.
PaxDbiQ8TEK3.
PRIDEiQ8TEK3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi84444.
GeneCardsiGC19P002115.
HGNCiHGNC:24948. DOT1L.
MIMi607375. gene.
neXtProtiNX_Q8TEK3.
PharmGKBiPA134993717.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG294902.
GeneTreeiENSGT00390000013515.
HOGENOMiHOG000143530.
HOVERGENiHBG051393.
InParanoidiQ8TEK3.
KOiK11427.
OMAiNGLPYQS.
OrthoDBiEOG7W6WJV.
PhylomeDBiQ8TEK3.
TreeFamiTF106393.

Miscellaneous databases

ChiTaRSiDOT1L. human.
EvolutionaryTraceiQ8TEK3.
GeneWikiiDOT1L.
GenomeRNAii84444.
NextBioi74205.
PROiQ8TEK3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TEK3.
CleanExiHS_DOT1L.
ExpressionAtlasiQ8TEK3. baseline and differential.
GenevestigatoriQ8TEK3.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR025789. DOT1_dom.
IPR013110. DOT1_dom_Pfam.
IPR021169. DOT1L/grappa.
IPR029063. SAM-dependent_MTases.
[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]
ProtoNetiSearch...

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: February 4, 2015
This is version 131 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.