Q8TEK3 (DOT1L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DOT1L
Synonyms:	KIAA1814, KMT4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1739 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA.
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.1
Subunit structure	Interacts with MLLT10. Ref.5 Ref.11
Subcellular location	Nucleus Probable.
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.
Sequence similarities	Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family. Contains 1 DOT1 domain.
Sequence caution	The sequence AAC08316.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	DNA-binding S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of JAK-STAT cascade Inferred from direct assay PubMed 22002246. Source: UniProtKB regulation of transcription regulatory region DNA binding Inferred from mutant phenotype PubMed 22002246. Source: UniProtKB
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone-lysine N-methyltransferase activity Inferred from direct assay PubMed 17707234. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MLLT1	Q03111	4	EBI-2619253,EBI-1384215

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q8TEK3-1)

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.

Isoform 1 (identifier: Q8TEK3-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1739

1739

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

PRO_0000186089

Regions

Domain

16 – 330

315

DOT1

Region

136 – 139

4

S-adenosyl-L-methionine binding

Region

159 – 168

10

S-adenosyl-L-methionine binding

Region

222 – 223

2

S-adenosyl-L-methionine binding

Region

391 – 416

26

Required for interaction with nucleosomes and DNA

Sites

Binding site

186

1

S-adenosyl-L-methionine

Amino acid modifications

Modified residue

374

1

Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10

Modified residue

471

1

Phosphoserine Ref.9

Modified residue

480

1

Phosphothreonine Ref.9

Modified residue

775

1

Phosphoserine Ref.7 Ref.9

Modified residue

834

1

Phosphoserine Ref.9

Modified residue

900

1

Phosphothreonine Ref.8

Modified residue

902

1

Phosphoserine Ref.8 Ref.9 Ref.10

Modified residue

1001

1

Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9

Modified residue

1009

1

Phosphoserine Ref.7

Modified residue

1035

1

Phosphoserine Ref.9

Modified residue

1213

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

1537

1

V → N in isoform 1.

VSP_002228

Alternative sequence

1538 – 1739

202

Missing in isoform 1.

VSP_002229

Natural variant

726

1

L → M.
Corresponds to variant rs880525 [ dbSNP | Ensembl ].

VAR_014287

Natural variant

1386

1

G → S.
Corresponds to variant rs3815308 [ dbSNP | Ensembl ].

VAR_014288

Natural variant

1418

1

V → L.
Corresponds to variant rs2302061 [ dbSNP | Ensembl ].

VAR_014289

Experimental info

Mutagenesis

163 – 165

3

GSG → RCR: Abolishes methyltransferase activity. Ref.1

Mutagenesis

241

1

N → A or D: Loss of activity. Ref.11

Mutagenesis

312

1

Y → A: Loss of activity. Ref.11

Mutagenesis

312

1

Y → F: No effect. Ref.11

Sequence conflict

210

1

G → E in BAB84946. Ref.4

Sequence conflict

454 – 467

14

RSPHS…LPPSV → TLRTPSGSPRRTKL Ref.3

Sequence conflict

464

1

P → L in BAB84946. Ref.4

Secondary structure

1

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1739

Helix Strand Turn

Details...

Beta strand

6 – 9

4

Beta strand

18 – 23

6

Beta strand

26 – 28

3

Helix

33 – 47

15

Helix

49 – 54

6

Helix

57 – 62

6

Helix

68 – 90

23

Beta strand

91 – 93

3

Beta strand

98 – 100

3

Helix

104 – 118

15

Helix

122 – 124

3

Helix

126 – 128

3

Beta strand

129 – 131

3

Helix

133 – 138

6

Helix

140 – 151

12

Beta strand

158 – 163

6

Helix

168 – 176

9

Beta strand

180 – 186

7

Helix

189 – 209

21

Beta strand

215 – 220

6

Helix

226 – 233

8

Beta strand

236 – 240

5

Turn

243 – 245

3

Helix

247 – 257

11

Beta strand

265 – 270

6

Beta strand

281 – 283

3

Helix

287 – 289

3

Beta strand

290 – 295

6

Beta strand

307 – 309

3

Beta strand

313 – 317

5

Helix

320 – 330

11

Helix

332 – 342

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified November 15, 2002. Version 2. Checksum: EBA575CE3C090CAC	FASTA	1,739	184,853
	10 20 30 40 50 60 MGEKLELRLK SPVGAEPAVY PWPLPVYDKH HDAAHEIIET IRWVCEEIPD LKLAMENYVL 70 80 90 100 110 120 IDYDTKSFES MQRLCDKYNR AIDSIHQLWK GTTQPMKLNT RPSTGLLRHI LQQVYNHSVT 130 140 150 160 170 180 DPEKLNNYEP FSPEVYGETS FDLVAQMIDE IKMTDDDLFV DLGSGVGQVV LQVAAATNCK 190 200 210 220 230 240 HHYGVEKADI PAKYAETMDR EFRKWMKWYG KKHAEYTLER GDFLSEEWRE RIANTSVIFV 250 260 270 280 290 300 NNFAFGPEVD HQLKERFANM KEGGRIVSSK PFAPLNFRIN SRNLSDIGTI MRVVELSPLK 310 320 330 340 350 360 GSVSWTGKPV SYYLHTIDRT ILENYFSSLK NPKLREEQEA ARRRQQRESK SNAATPTKGP 370 380 390 400 410 420 EGKVAGPADA PMDSGAEEEK AGAATVKKPS PSKARKKKLN KKGRKMAGRK RGRPKKMNTA 430 440 450 460 470 480 NPERKPKKNQ TALDALHAQT VSQTAASSPQ DAYRSPHSPF YQLPPSVQRH SPNPLLVAPT 490 500 510 520 530 540 PPALQKLLES FKIQYLQFLA YTKTPQYKAS LQELLGQEKE KNAQLLGAAQ QLLSHCQAQK 550 560 570 580 590 600 EEIRRLFQQK LDELGVKALT YNDLIQAQKE ISAHNQQLRE QSEQLEQDNR ALRGQSLQLL 610 620 630 640 650 660 KARCEELQLD WATLSLEKLL KEKQALKSQI SEKQRHCLEL QISIVELEKS QRQQELLQLK 670 680 690 700 710 720 SCVPPDDALS LHLRGKGALG RELEPDASRL HLELDCTKFS LPHLSSMSPE LSMNGQAAGY 730 740 750 760 770 780 ELCGVLSRPS SKQNTPQYLA SPLDQEVVPC TPSHVGRPRL EKLSGLAAPD YTRLSPAKIV 790 800 810 820 830 840 LRRHLSQDHT VPGRPAASEL HSRAEHTKEN GLPYQSPSVP GSMKLSPQDP RPLSPGALQL 850 860 870 880 890 900 AGEKSSEKGL RERAYGSSGE LITSLPISIP LSTVQPNKLP VSIPLASVVL PSRAERARST 910 920 930 940 950 960 PSPVLQPRDP SSTLEKQIGA NAHGAGSRSL ALAPAGFSYA GSVAISGALA GSPASLTPGA 970 980 990 1000 1010 1020 EPATLDESSS SGSLFATVGS RSSTPQHPLL LAQPRNSLPA SPAHQLSSSP RLGGAAQGPL 1030 1040 1050 1060 1070 1080 PEASKGDLPS DSGFSDPESE AKRRIVFTIT TGAGSAKQSP SSKHSPLTAS ARGDCVPSHG 1090 1100 1110 1120 1130 1140 QDSRRRGRRK RASAGTPSLS AGVSPKRRAL PSVAGLFTQP SGSPLNLNSM VSNINQPLEI 1150 1160 1170 1180 1190 1200 TAISSPETSL KSSPVPYQDH DQPPVLKKER PLSQTNGAHY SPLTSDEEPG SEDEPSSARI 1210 1220 1230 1240 1250 1260 ERKIATISLE SKSPPKTLEN GGGLAGRKPA PAGEPVNSSK WKSTFSPISD IGLAKSADSP 1270 1280 1290 1300 1310 1320 LQASSALSQN SLFTFRPALE EPSADAKLAA HPRKGFPGSL SGADGLSPGT NPANGCTFGG 1330 1340 1350 1360 1370 1380 GLAADLSLHS FSDGASLPHK GPEAAGLSSP LSFPSQRGKE GSDANPFLSK RQLDGLAGLK 1390 1400 1410 1420 1430 1440 GEGSRGKEAG EGGLPLCGPT DKTPLLSGKA AKARDREVDL KNGHNLFISA AAVPPGSLLS 1450 1460 1470 1480 1490 1500 GPGLAPAASS AGGAASSAQT HRSFLGPFPP GPQFALGPMS LQANLGSVAG SSVLQSLFSS 1510 1520 1530 1540 1550 1560 VPAAAGLVHV SSAATRLTNS HAMGSFSGVA GGTVGGVVFN HAVPSASAHP FGARVGRGAA 1570 1580 1590 1600 1610 1620 CGSATLGPSP LQAAASASAS SFQAPASVET RPPPPPPPPP PPLPPPAHLG RSPAGPPVLH 1630 1640 1650 1660 1670 1680 APPPPNAALP PPPTLLASNP EPALLQSLAS LPPNQAFLPP TSAASLPPAN ASLSIKLTSL 1690 1700 1710 1720 1730 PHKGARPSFT VHHQPLPRLA LAQAAPGIPQ ASATGPSAVW VSLGMPPPYA AHLSGVKPR
	Isoform 1 [UniParc]. Checksum: 9CEA12850DC4ACB1	FASTA	1,537	164,856
	10 20 30 40 50 60 MGEKLELRLK SPVGAEPAVY PWPLPVYDKH HDAAHEIIET IRWVCEEIPD LKLAMENYVL 70 80 90 100 110 120 IDYDTKSFES MQRLCDKYNR AIDSIHQLWK GTTQPMKLNT RPSTGLLRHI LQQVYNHSVT 130 140 150 160 170 180 DPEKLNNYEP FSPEVYGETS FDLVAQMIDE IKMTDDDLFV DLGSGVGQVV LQVAAATNCK 190 200 210 220 230 240 HHYGVEKADI PAKYAETMDR EFRKWMKWYG KKHAEYTLER GDFLSEEWRE RIANTSVIFV 250 260 270 280 290 300 NNFAFGPEVD HQLKERFANM KEGGRIVSSK PFAPLNFRIN SRNLSDIGTI MRVVELSPLK 310 320 330 340 350 360 GSVSWTGKPV SYYLHTIDRT ILENYFSSLK NPKLREEQEA ARRRQQRESK SNAATPTKGP 370 380 390 400 410 420 EGKVAGPADA PMDSGAEEEK AGAATVKKPS PSKARKKKLN KKGRKMAGRK RGRPKKMNTA 430 440 450 460 470 480 NPERKPKKNQ TALDALHAQT VSQTAASSPQ DAYRSPHSPF YQLPPSVQRH SPNPLLVAPT 490 500 510 520 530 540 PPALQKLLES FKIQYLQFLA YTKTPQYKAS LQELLGQEKE KNAQLLGAAQ QLLSHCQAQK 550 560 570 580 590 600 EEIRRLFQQK LDELGVKALT YNDLIQAQKE ISAHNQQLRE QSEQLEQDNR ALRGQSLQLL 610 620 630 640 650 660 KARCEELQLD WATLSLEKLL KEKQALKSQI SEKQRHCLEL QISIVELEKS QRQQELLQLK 670 680 690 700 710 720 SCVPPDDALS LHLRGKGALG RELEPDASRL HLELDCTKFS LPHLSSMSPE LSMNGQAAGY 730 740 750 760 770 780 ELCGVLSRPS SKQNTPQYLA SPLDQEVVPC TPSHVGRPRL EKLSGLAAPD YTRLSPAKIV 790 800 810 820 830 840 LRRHLSQDHT VPGRPAASEL HSRAEHTKEN GLPYQSPSVP GSMKLSPQDP RPLSPGALQL 850 860 870 880 890 900 AGEKSSEKGL RERAYGSSGE LITSLPISIP LSTVQPNKLP VSIPLASVVL PSRAERARST 910 920 930 940 950 960 PSPVLQPRDP SSTLEKQIGA NAHGAGSRSL ALAPAGFSYA GSVAISGALA GSPASLTPGA 970 980 990 1000 1010 1020 EPATLDESSS SGSLFATVGS RSSTPQHPLL LAQPRNSLPA SPAHQLSSSP RLGGAAQGPL 1030 1040 1050 1060 1070 1080 PEASKGDLPS DSGFSDPESE AKRRIVFTIT TGAGSAKQSP SSKHSPLTAS ARGDCVPSHG 1090 1100 1110 1120 1130 1140 QDSRRRGRRK RASAGTPSLS AGVSPKRRAL PSVAGLFTQP SGSPLNLNSM VSNINQPLEI 1150 1160 1170 1180 1190 1200 TAISSPETSL KSSPVPYQDH DQPPVLKKER PLSQTNGAHY SPLTSDEEPG SEDEPSSARI 1210 1220 1230 1240 1250 1260 ERKIATISLE SKSPPKTLEN GGGLAGRKPA PAGEPVNSSK WKSTFSPISD IGLAKSADSP 1270 1280 1290 1300 1310 1320 LQASSALSQN SLFTFRPALE EPSADAKLAA HPRKGFPGSL SGADGLSPGT NPANGCTFGG 1330 1340 1350 1360 1370 1380 GLAADLSLHS FSDGASLPHK GPEAAGLSSP LSFPSQRGKE GSDANPFLSK RQLDGLAGLK 1390 1400 1410 1420 1430 1440 GEGSRGKEAG EGGLPLCGPT DKTPLLSGKA AKARDREVDL KNGHNLFISA AAVPPGSLLS 1450 1460 1470 1480 1490 1500 GPGLAPAASS AGGAASSAQT HRSFLGPFPP GPQFALGPMS LQANLGSVAG SSVLQSLFSS 1510 1520 1530 VPAAAGLVHV SSAATRLTNS HAMGSFSGVA GGTVGGN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
[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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-775; SER-1001 AND SER-1009, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY.
[11]	"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, MASS SPECTROMETRY, MUTAGENESIS OF ASN-241 AND TYR-312, NUCLEOSOME BINDING, INTERACTION WITH DNA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF509504 mRNA. Translation: AAM88322.1.
AC004490 Genomic DNA. Translation: AAC08316.1. Sequence problems.
AB058717 mRNA. Translation: BAB47443.1.
AK074120 mRNA. Translation: BAB84946.1.

IPI

IPI00289034.
IPI00873164.

RefSeq

NP_115871.1. NM_032482.2.

UniGene

Hs.713641.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q8TEK3.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-56410N.

IntAct

Q8TEK3. 2 interactions.

STRING

9606.ENSP00000381657.

PTM databases

PhosphoSite

Q8TEK3.

Polymorphism databases

DMDM

25090171.

Proteomic databases

PaxDb

Q8TEK3.

PRIDE

Q8TEK3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000398665; ENSP00000381657; ENSG00000104885.

GeneID

84444.

KEGG

hsa:84444.

UCSC

uc002lvb.4. human.
uc002lvc.1. human.

Organism-specific databases

CTD

84444.

GeneCards

GC19P002115.

HGNC

HGNC:24948. DOT1L.

MIM

607375. gene.

neXtProt

NX_Q8TEK3.

PharmGKB

PA134993717.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG294902.

HOGENOM

HOG000143530.

HOVERGEN

HBG051393.

InParanoid

Q8TEK3.

KO

K11427.

Gene expression databases

ArrayExpress

Q8TEK3.

Bgee

Q8TEK3.

CleanEx

HS_DOT1L.

Genevestigator

Q8TEK3.

GermOnline

ENSG00000104885. Homo sapiens.

Family and domain databases

InterPro

IPR017956. AT_hook_DNA-bd_motif.
IPR013110. DOT1.
IPR025789. Histone_H3-K79_MeTrfase.
IPR021169. Histone_H3-K79_MeTrfase_met.
[Graphical view]

Pfam

PF08123. DOT1. 1 hit.
[Graphical view]

PIRSF

PIRSF037123. Histone_H3-K79_MeTrfase_met. 1 hit.

SMART

SM00384. AT_hook. 1 hit.
[Graphical view]

PROSITE

PS51569. DOT1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1795117.

ChiTaRS

DOT1L. human.

EvolutionaryTrace

Q8TEK3.

GenomeRNAi

84444.

NextBio

74205.

SOURCE

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Entry information

Entry name

DOT1L_HUMAN

Accession

Primary (citable) accession number: Q8TEK3
Secondary accession number(s): O60379, Q96JL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	November 15, 2002
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.