UniProtKB - Q03164 (KMT2A_HUMAN)

>sp|Q03164|KMT2A_HUMAN Histone-lysine N-methyltransferase 2A OS=Homo sapiens OX=9606 GN=KMT2A PE=1 SV=5
MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAV
AAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSA
AIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPR
SGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKD
ISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIV
RRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRI
IPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSR
IIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSS
SPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGS
RTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPAS
TAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPED
VGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSN
RTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSL
SISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFT
PGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQ
SSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKI
LIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTD
KRVASLLKKAKAQLCKIEKSKSLKQTDQPKAQGQESDSSETSVRGPRIKHVCRRAAVALG
RKRAVFPDDMPTLSALPWEEREKILSSMGNDDKSSIAGSEDAEPLAPPIKPIKPVTRNKA
PQEPPVKKGRRSRRCGQCPGCQVPEDCGVCTNCLDKPKFGGRNIKKQCCKMRKCQNLQWM
PSKAYLQKQAKAVKKKEKKSKTSEKKDSKESSVVKNVVDSSQKPTPSAREDPAPKKSSSE
PPPRKPVEEKSEEGNVSAPGPESKQATTPASRKSSKQVSQPALVIPPQPPTTGPPRKEVP
KTTPSEPKKKQPPPPESGPEQSKQKKVAPRPSIPVKQKPKEKEKPPPVNKQENAGTLNIL
STLSNGNSSKQKIPADGVHRIRVDFKEDCEAENVWEMGGLGILTSVPITPRVVCFLCASS
GHVEFVYCQVCCEPFHKFCLEENERPLEDQLENWCCRRCKFCHVCGRQHQATKQLLECNK
CRNSYHPECLGPNYPTKPTKKKKVWICTKCVRCKSCGSTTPGKGWDAQWSHDFSLCHDCA
KLFAKGNFCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYT
CVNCTERHPAEWRLALEKELQISLKQVLTALLNSRTTSHLLRYRQAAKPPDLNPETEESI
PSRSSPEGPDPPVLTEVSKQDDQQPLDLEGVKRKMDQGNYTSVLEFSDDIVKIIQAAINS
DGGQPEIKKANSMVKSFFIRQMERVFPWFSVKKSRFWEPNKVSSNSGMLPNAVLPPSLDH
NYAQWQEREENSHTEQPPLMKKIIPAPKPKGPGEPDSPTPLHPPTPPILSTDRSREDSPE
LNPPPGIEDNRQCALCLTYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKN
VHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLDDKKVYCQRHRDL
IKGEVVPENGFEVFRRVFVDFEGISLRRKFLNGLEPENIHMMIGSMTIDCLGILNDLSDC
EDKLFPIGYQCSRVYWSTTDARKRCVYTCKIVECRPPVVEPDINSTVEHDENRTIAHSPT
SFTESSSKESQNTAEIISPPSPDRPPHSQTSGSCYYHVISKVPRIRTPSYSPTQRSPGCR
PLPSAGSPTPTTHEIVTVGDPLLSSGLRSIGSRRHSTSSLSPQRSKLRIMSPMRTGNTYS
RNNVSSVSTTGTATDLESSAKVVDHVLGPLNSSTSLGQNTSTSSNLQRTVVTVGNKNSHL
DGSSSSEMKQSSASDLVSKSSSLKGEKTKVLSSKSSEGSAHNVAYPGIPKLAPQVHNTTS
RELNVSKIGSFAEPSSVSFSSKEALSFPHLHLRGQRNDRDQHTDSTQSANSSPDEDTEVK
TLKLSGMSNRSSIINEHMGSSSRDRRQKGKKSCKETFKEKHSSKSFLEPGQVTTGEEGNL
KPEFMDEVLTPEYMGQRPCNNVSSDKIGDKGLSMPGVPKAPPMQVEGSAKELQAPRKRTV
KVTLTPLKMENESQSKNALKESSPASPLQIESTSPTEPISASENPGDGPVAQPSPNNTSC
QDSQSNNYQNLPVQDRNLMLPDGPKPQEDGSFKRRYPRRSARARSNMFFGLTPLYGVRSY
GEEDIPFYSSSTGKKRGKRSAEGQVDGADDLSTSDEDDLYYYNFTRTVISSGGEERLASH
NLFREEEQCDLPKISQLDGVDDGTESDTSVTATTRKSSQIPKRNGKENGTENLKIDRPED
AGEKEHVTKSSVGHKNEPKMDNCHSVSRVKTQGQDSLEAQLSSLESSRRVHTSTPSDKNL
LDTYNTELLKSDSDNNNSDDCGNILPSDIMDFVLKNTPSMQALGESPESSSSELLNLGEG
LGLDSNREKDMGLFEVFSQQLPTTEPVDSSVSSSISAEEQFELPLELPSDLSVLTTRSPT
VPSQNPSRLAVISDSGEKRVTITEKSVASSESDPALLSPGVDPTPEGHMTPDHFIQGHMD
ADHISSPPCGSVEQGHGNNQDLTRNSSTPGLQVPVSPTVPIQNQKYVPNSTDSPGPSQIS
NAAVQTTPPHLKPATEKLIVVNQNMQPLYVLQTLPNGVTQKIQLTSSVSSTPSVMETNTS
VLGPMGGGLTLTTGLNPSLPTSQSLFPSASKGLLPMSHHQHLHSFPAATQSSFPPNISNP
PSGLLIGVQPPPDPQLLVSESSQRTDLSTTVATPSSGLKKRPISRLQTRKNKKLAPSSTP
SNIAPSDVVSNMTLINFTPSQLPNHPSLLDLGSLNTSSHRTVPNIIKRSKSSIMYFEPAP
LLPQSVGGTAATAAGTSTISQDTSHLTSGSVSGLASSSSVLNVVSMQTTTTPTSSASVPG
HVTLTNPRLLGTPDIGSISNLLIKASQQSLGIQDQPVALPPSSGMFPQLGTSQTPSTAAI
TAASSICVLPSTQTTGITAASPSGEADEHYQLQHVNQLLASKTGIHSSQRDLDSASGPQV
SNFTQTVDAPNSMGLEQNKALSSAVQASPTSPGGSPSSPSSGQRSASPSVPGPTKPKPKT
KRFQLPLDKGNGKKHKVSHLRTSSSEAHIPDQETTSLTSGTGTPGAEAEQQDTASVEQSS
QKECGQPAGQVAVLPEVQVTQNPANEQESAEPKTVEEEESNFSSPLMLWLQQEQKRKESI
TEKKPKKGLVFEISSDDGFQICAESIEDAWKSLTDKVQEARSNARLKQLSFAGVNGLRML
GILHDAVVFLIEQLSGAKHCRNYKFRFHKPEEANEPPLNPHGSARAEVHLRKSAFDMFNF
LASKHRQPPEYNPNDEEEEEVQLKSARRATSMDLPMPMRFRHLKKTSKEAVGVYRSPIHG
RGLFCKRNIDAGEMVIEYAGNVIRSIQTDKREKYYDSKGIGCYMFRIDDSEVVDATMHGN
AARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCG
AKKCRKFLN

Entry version 240 (17 Jun 2020)
Sequence version 5 (01 May 2007)
Previous versions | rss

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Protein

Histone-lysine N-methyltransferase 2A

Gene

KMT2A

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation (PubMed:12453419, PubMed:20677832, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20677832, PubMed:20010842). Promotes PPP1R15A-induced apoptosis. Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-ARNTL/BMAL1 heterodimer. Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-ARNTL/BMAL1 to chromatin (By similarity).By similarity1 Publication8 Publications

Catalytic activityⁱ

L-lysyl⁴-[histone H3]
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+ 3
S-adenosyl-L-methionine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
= 3
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁶,N⁶,N⁶-trimethyl-L-lysyl⁴-[histone H3]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+ 3
S-adenosyl-L-homocysteine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.25
  "ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation."
  Nakamura T., Mori T., Tada S., Krajewski W., Rozovskaia T., Wassell R., Dubois G., Mazo A., Croce C.M., Canaani E.
  Mol. Cell 10:1119-1128(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY.
- Ref.54
  "Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks."
  Southall S.M., Wong P.S., Odho Z., Roe S.M., Wilson J.R.
  Mol. Cell 33:181-191(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3785-3969 IN COMPLEX WITH ZINC; S-ADENOSYL-L-HOMOCYSTEINE AND HISTONE H3 PEPTIDE, FUNCTION, CATALYTIC ACTIVITY, DOMAIN SET, INTERACTION WITH ASH2L AND RBBP5, MUTAGENESIS OF TYR-3858; GLN-3867; ASP-3869; ARG-3871; GLU-3872; TYR-3874; LYS-3878 AND TYR-3942.
- Ref.65
  "Structural basis for activity regulation of MLL family methyltransferases."
  Li Y., Han J., Zhang Y., Cao F., Liu Z., Li S., Wu J., Hu C., Wang Y., Shuai J., Chen J., Cao L., Li D., Shi P., Tian C., Zhang J., Dou Y., Li G., Chen Y., Lei M.
  Nature 530:447-452(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3813-3969 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF ASN-3861; ARG-3864 AND GLN-3867.
EC:
2.1.1.354
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.25
  "ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation."
  Nakamura T., Mori T., Tada S., Krajewski W., Rozovskaia T., Wassell R., Dubois G., Mazo A., Croce C.M., Canaani E.
  Mol. Cell 10:1119-1128(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY.
- Ref.54
  "Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks."
  Southall S.M., Wong P.S., Odho Z., Roe S.M., Wilson J.R.
  Mol. Cell 33:181-191(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3785-3969 IN COMPLEX WITH ZINC; S-ADENOSYL-L-HOMOCYSTEINE AND HISTONE H3 PEPTIDE, FUNCTION, CATALYTIC ACTIVITY, DOMAIN SET, INTERACTION WITH ASH2L AND RBBP5, MUTAGENESIS OF TYR-3858; GLN-3867; ASP-3869; ARG-3871; GLU-3872; TYR-3874; LYS-3878 AND TYR-3942.
- Ref.65
  "Structural basis for activity regulation of MLL family methyltransferases."
  Li Y., Han J., Zhang Y., Cao F., Liu Z., Li S., Wu J., Hu C., Wang Y., Shuai J., Chen J., Cao L., Li D., Shi P., Tian C., Zhang J., Dou Y., Li G., Chen Y., Lei M.
  Nature 530:447-452(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3813-3969 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF ASN-3861; ARG-3864 AND GLN-3867.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
L-lysyl⁴-[histone H3]
L-lysine residue
zoom
+
3
S-adenosyl-L-methionine
zoom
=
3
H⁺
+
N⁶,N⁶,N⁶-trimethyl-L-lysyl⁴-[histone H3]
N⁶,N⁶,N⁶-trimethyl-L-lysine residue
zoom
+
3
S-adenosyl-L-homocysteine
zoom

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	1155	ZincCombined sources1 Publication	1
Metal bindingⁱ	1158	ZincCombined sources1 Publication	1
Metal bindingⁱ	1161	ZincCombined sources1 Publication	1
Metal bindingⁱ	1167	ZincCombined sources1 Publication	1
Metal bindingⁱ	1170	ZincCombined sources1 Publication	1
Metal bindingⁱ	1173	ZincCombined sources1 Publication	1
Metal bindingⁱ	1189	ZincCombined sources1 Publication	1
Metal bindingⁱ	1194	ZincCombined sources1 Publication	1
Siteⁱ	3765	Important for WDR5-recognition and binding1 Publication	1
Binding siteⁱ	3839	S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources2 Publications	1
Binding siteⁱ	3841	S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources2 Publications	1
Binding siteⁱ	3883	S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	3909	ZincCombined sources2 Publications	1
Metal bindingⁱ	3957	ZincCombined sources2 Publications	1
Binding siteⁱ	3958	S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	3959	ZincCombined sources2 Publications	1
Metal bindingⁱ	3964	ZincCombined sources2 Publications	1

Regions

Feature key	Position(s)	DescriptionActions	Length
DNA bindingⁱ	169 – 180	A.T hook 1Add BLAST	12
DNA bindingⁱ	217 – 227	A.T hook 2Add BLAST	11
DNA bindingⁱ	301 – 309	A.T hook 3	9
Zinc fingerⁱ	1147 – 1195	CXXC-typePROSITE-ProRule annotation1 PublicationAdd BLAST	49
Zinc fingerⁱ	1431 – 1482	PHD-type 1PROSITE-ProRule annotationAdd BLAST	52
Zinc fingerⁱ	1479 – 1533	PHD-type 2PROSITE-ProRule annotationAdd BLAST	55
Zinc fingerⁱ	1566 – 1627	PHD-type 3PROSITE-ProRule annotationAdd BLAST	62
Zinc fingerⁱ	1870 – 1910	C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST	41
Zinc fingerⁱ	1931 – 1978	PHD-type 4PROSITE-ProRule annotationAdd BLAST	48

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chromatin regulator, DNA-binding, Methyltransferase, Transferase
Biological process	Apoptosis, Biological rhythms, Transcription, Transcription regulation
Ligand	Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-HSA-3214841 PKMTs methylate histone lysines R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs R-HSA-9616222 Transcriptional regulation of granulopoiesis
SIGNORⁱ	Q03164

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Histone-lysine N-methyltransferase 2A (EC:2.1.1.3543 Publications) Short name: Lysine N-methyltransferase 2A Alternative name(s): ALL-11 Publication CXXC-type zinc finger protein 7 Myeloid/lymphoid or mixed-lineage leukemia Myeloid/lymphoid or mixed-lineage leukemia protein 1 Trithorax-like protein Zinc finger protein HRX Cleaved into the following 2 chains: MLL cleavage product N320 Alternative name(s): N-terminal cleavage product of 320 kDa Short name: p320 MLL cleavage product C180 Alternative name(s): C-terminal cleavage product of 180 kDa Short name: p180
Gene namesⁱ	Name:KMT2A Synonyms:ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 11

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000118058.20
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:7132 KMT2A
MIMⁱ	159555 gene+phenotype
neXtProtⁱ	NX_Q03164

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Wiedemann-Steiner syndrome (WDSTS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA syndrome characterized by hairy elbows (hypertrichosis cubiti), intellectual disability, a distinctive facial appearance, and short stature. Facial characteristics include long eyelashes, thick or arched eyebrows with a lateral flare, and downslanting and vertically narrow palpebral fissures.

Related information in OMIM

Chromosomal aberrations involving KMT2A are a cause of acute leukemias. Translocation t(1;11)(q21;q23) with MLLT11/AF1Q; translocation t(3;11)(p21;q23) with NCKIPSD/AF3p21; translocation t(3,11)(q25,q23) with GMPS; translocation t(4;11)(q21;q23) with AFF1/MLLT2/AF4; insertion ins(5;11)(q31;q13q23) with AFF4/AF5Q31; translocation t(5;11)(q12;q23) with AF5-alpha/CENPK; translocation t(6;11)(q27;q23) with AFDN; translocation t(9;11)(p22;q23) with MLLT3/AF9; translocation t(10;11)(p11.2;q23) with ABI1; translocation t(10;11)(p12;q23) with MLLT10/AF10; t(11;15)(q23;q14) with KNL1 and ZFYVE19; translocation t(11;17)(q23;q21) with MLLT6/AF17; translocation t(11;19)(q23;p13.3) with ELL; translocation t(11;19)(q23;p13.3) with MLLT1/ENL; translocation t(11;19)(q23;p23) with GAS7; translocation t(X;11)(q13;q23) with FOXO4/AFX1. Translocation t(3;11)(q28;q23) with LPP. Translocation t(10;11)(q22;q23) with TET1. Translocation t(9;11)(q34;q23) with DAB2IP. Translocation t(4;11)(p12;q23) with FRYL. Fusion proteins KMT2A-MLLT1, KMT2A-MLLT3 and KMT2A-ELL interact with PPP1R15A and, on the contrary to unfused KMT2A, inhibit PPP1R15A-induced apoptosis. Fusion protein KMT2A-MLLT3 interacts with MEN1 and PSIP1 (PubMed:22936661, PubMed:25305204).3 Publications

A chromosomal aberration involving KMT2A may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with SEPT11.1 Publication

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	6	R → A: Reduced interaction with MEN1. 1 Publication	1
Mutagenesisⁱ	7	W → A: Reduced interaction with MEN1. 1 Publication	1
Mutagenesisⁱ	8	R → A: Reduced interaction with MEN1. 1 Publication	1
Mutagenesisⁱ	9	F → A: Loss of interaction with MEN1. 1 Publication	1
Mutagenesisⁱ	9	F → H or Y: Reduced interaction with MEN1. 1 Publication	1
Mutagenesisⁱ	10	P → A: Reduced interaction with MEN1. 1 Publication	1
Mutagenesisⁱ	11	A → R: Reduced interaction with MEN1. 1 Publication	1
Mutagenesisⁱ	12	R → A: Reduced interaction with MEN1. 1 Publication	1
Mutagenesisⁱ	13	P → A: Reduced interaction with MEN1. 1 Publication	1
Mutagenesisⁱ	24	R → E: Reduced interaction with MEN1; when associated with E-25. 1 Publication	1
Mutagenesisⁱ	25	R → E: Reduced interaction with MEN1; when associated with E-24. 1 Publication	1
Mutagenesisⁱ	129	F → A: Weakly affects interaction with PSIP1 whereas significantly decreases interaction of KMT2A-MEN1 complex with PSIP1. Reduced interaction with PSIP1; when associated with A-133. 2 Publications	1
Mutagenesisⁱ	132	V → A: Reduced interaction with PSIP1; when associated with A-133. 1 Publication	1
Mutagenesisⁱ	133	F → A: Reduced interaction with PSIP1; when associated with A-129 or A-132. 2 Publications	1
Mutagenesisⁱ	136	S → D: Phosphomimetic mutant. Significant increase in interaction with PSIP1; when associated with D-142. 1 Publication	1
Mutagenesisⁱ	142	S → D: Phosphomimetic mutant. Significant increase in interaction with PSIP1; when associated with D-136. 1 Publication	1
Mutagenesisⁱ	144	E → Q: Loss of interaction with PSIP1; when associated with Q-146 and A-148. 1 Publication	1
Mutagenesisⁱ	146	E → Q: Loss of interaction with PSIP1; when associated with Q-144 and A-148. 1 Publication	1
Mutagenesisⁱ	148	F → A: Reduced interaction with PSIP1. Loss of interaction with PSIP1; when associated with A-149 or Q-144 and Q-146. 2 Publications	1
Mutagenesisⁱ	149	L → A: Loss of interaction with PSIP1; when associated with A-148. 1 Publication	1
Mutagenesisⁱ	151	F → A: Reduced interaction with PSIP1. 1 Publication	1
Mutagenesisⁱ	1150	R → A: Impairs DNA-binding. 1 Publication	1
Mutagenesisⁱ	1151	R → A: Impairs DNA-binding. 1 Publication	1
Mutagenesisⁱ	1153	R → A: No effect on stability or DNA-binding. 1 Publication	1
Mutagenesisⁱ	1154	R → A: Impairs DNA-binding. 2 Publications	1
Mutagenesisⁱ	1155	C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	1
Mutagenesisⁱ	1158	C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	1
Mutagenesisⁱ	1161	C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	1
Mutagenesisⁱ	1162	Q → A: No effect on stability or DNA-binding. 1 Publication	1
Mutagenesisⁱ	1166	D → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	1
Mutagenesisⁱ	1167	C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	1
Mutagenesisⁱ	1170	C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	1
Mutagenesisⁱ	1172	N → A: No effect on stability or DNA-binding. 1 Publication	1
Mutagenesisⁱ	1173	C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	1
Mutagenesisⁱ	1175	D → A: Impairs DNA-binding. 1 Publication	1
Mutagenesisⁱ	1176	K → A: Impairs DNA-binding. 1 Publication	1
Mutagenesisⁱ	1178 – 1181	KFGG → AAAA: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	4
Mutagenesisⁱ	1178	K → A: Impairs DNA-binding. 1 Publication	1
Mutagenesisⁱ	1179	F → A: Impairs DNA-binding. 1 Publication	1
Mutagenesisⁱ	1183	N → A: Impairs DNA-binding. 1 Publication	1
Mutagenesisⁱ	1185	K → A: Impairs DNA-binding. 2 Publications	1
Mutagenesisⁱ	1186	K → A: Impairs DNA-binding. 1 Publication	1
Mutagenesisⁱ	1187	Q → A: Impairs DNA-binding. 2 Publications	1
Mutagenesisⁱ	1188	C → A: No effect on stability or DNA-binding. 2 Publications	1
Mutagenesisⁱ	1188	C → D: Abolishes DNA-binding and increases CpG methylation of the HOXA9 promoter region. Does not lead to the development of leukemia when overexpressed in mice as gene fusion with MLLT3. 1 Publication	1
Mutagenesisⁱ	1189	C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	1
Mutagenesisⁱ	1192	R → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	1
Mutagenesisⁱ	1193	K → A: Impairs DNA-binding. 2 Publications	1
Mutagenesisⁱ	1194	C → A: Impairs zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication	1
Mutagenesisⁱ	1195	Q → A: No effect on stability or DNA-binding. 1 Publication	1
Mutagenesisⁱ	1196	N → A: No effect on stability or DNA-binding. 1 Publication	1
Mutagenesisⁱ	1197	L → A: Mildly decreases DNA-binding. 1 Publication	1
Mutagenesisⁱ	1200	M → A: No effect on DNA-binding. 1 Publication	1
Mutagenesisⁱ	1581	Y → A: Decreases affinity for histone H3K4me3. 1 Publication	1
Mutagenesisⁱ	1587	Q → A: Decreases affinity for histone H3K4me3. 1 Publication	1
Mutagenesisⁱ	1594	W → A: Abolishes interaction with histone H3K4me3. 1 Publication	1
Mutagenesisⁱ	1594	W → E: Decreases affinity for histone H3K4me3. 1 Publication	1
Mutagenesisⁱ	1617	V → A: Decreases binding affinity for PPIE. 1 Publication	1
Mutagenesisⁱ	1619	Y → A: May perturb protein folding and thereby decrease binding affinity for PPIE. 1 Publication	1
Mutagenesisⁱ	2666 – 2667	DG → AA: Reduces cleavage without abolishing it. Abolishes cleavage by TASP1; when associated with 2718-A--A-2720. 1 Publication	2
Mutagenesisⁱ	2718 – 2720	DGV → AAA: Abolishes cleavage by TASP1; when associated with 2666-A-A-2667. 2 Publications	3
Mutagenesisⁱ	3763	S → A: Increased interaction with WDR5. 1 Publication	1
Mutagenesisⁱ	3765	R → A: Loss of interaction with the WRAD complex and WDR5. 2 Publications	1
Mutagenesisⁱ	3769	H → A or F: Slight decrease in interaction with WDR5. 1 Publication	1
Mutagenesisⁱ	3769	H → Y: Increased interaction with WDR5. 1 Publication	1
Mutagenesisⁱ	3858	Y → A: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. 1 Publication	1
Mutagenesisⁱ	3858	Y → F: Slightly affects methyltransferase activity toward unmodified or monomethylated H3K4me. 1 Publication	1
Mutagenesisⁱ	3861	N → I: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with L-3867. 1 Publication	1
Mutagenesisⁱ	3861	N → T: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with V-3867. 1 Publication	1
Mutagenesisⁱ	3864	R → A: Disrupts interaction with ASH2L and RBBP5 and nearly abolishes histone methyltransferase activity. 1 Publication	1
Mutagenesisⁱ	3867	Q → A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3871. 1 Publication	1
Mutagenesisⁱ	3867	Q → L: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with I-3861. 1 Publication	1
Mutagenesisⁱ	3867	Q → V: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with T-3861. 1 Publication	1
Mutagenesisⁱ	3869	D → A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3872. 1 Publication	1
Mutagenesisⁱ	3871	R → A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3867. 1 Publication	1
Mutagenesisⁱ	3872	E → A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3869. 1 Publication	1
Mutagenesisⁱ	3874	Y → A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3878. 1 Publication	1
Mutagenesisⁱ	3878	K → A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3874. 1 Publication	1
Mutagenesisⁱ	3906	N → A: Loss of the histone H3 methyltransferase activity. 1 Publication	1
Mutagenesisⁱ	3942	Y → A or F: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. 2 Publications	1
Mutagenesisⁱ	3942	Y → F: Shifts from a specific monomethyltransferase to a di- and trimethyltransferase activity. 2 Publications	1

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	1334 – 1335	Breakpoint for translocation to form KMT2A-ZFYVE19 oncogene	2
Siteⁱ	1362 – 1363	Breakpoint for translocation to form KMT2A-AF3P21 and KMT2A-KNL1 oncogenes	2
Siteⁱ	1362 – 1363	Breakpoint for translocation to form KMT2A-CENPK oncogene	2
Siteⁱ	1362	Breakpoint for translocation to form KMT2A-FRYL fusion protein	1
Siteⁱ	1406 – 1407	Breakpoint for translocation to form KMT2A-AFF4 fusion protein	2
Siteⁱ	1444 – 1445	Breakpoint for translocation to form KMT2A-GAS7 oncogene	2
Siteⁱ	1444 – 1445	Breakpoint for translocation to form KMT2A-LPP	2

Keywords - Diseaseⁱ

Proto-oncogene

Organism-specific databases

DisGeNET More...DisGeNETⁱ	4297
MalaCards human disease database More...MalaCardsⁱ	KMT2A
MIMⁱ	159555 gene+phenotype 605130 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000118058
Orphanetⁱ	98831 Acute myeloid leukemia with 11q23 abnormalities 402017 Acute myeloid leukemia with t(9;11)(p22;q23) 98835 Acute undifferentiated leukemia 199 Cornelia de Lange syndrome 530995 Mixed phenotype acute leukemia 99860 Precursor B-cell acute lymphoblastic leukemia 319182 Wiedemann-Steiner syndrome
PharmGKBⁱ	PA241

Miscellaneous databases

Pharosⁱ	Q03164 Tchem

Pharosⁱ

Q03164 Tchem

Chemistry databases

ChEMBLⁱ	CHEMBL1293299

ChEMBLⁱ

CHEMBL1293299

Polymorphism and mutation databases

BioMutaⁱ	KMT2A
DMDMⁱ	146345435

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
ChainⁱPRO_0000124876	1 – 3969	Histone-lysine N-methyltransferase 2AAdd BLAST	3969
ChainⁱPRO_0000390949	1 – 2718	MLL cleavage product N320Add BLAST	2718
ChainⁱPRO_0000390950	2719 – 3969	MLL cleavage product C180Add BLAST	1251

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	136	Phosphoserine; by CK21 Publication	1
Modified residueⁱ	142	Phosphoserine; by CK21 Publication	1
Modified residueⁱ	153	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	197	PhosphoserineCombined sources	1
Modified residueⁱ	239	N6-acetyllysineBy similarity	1
Modified residueⁱ	373	N6-acetyllysineBy similarity	1
Modified residueⁱ	518	PhosphoserineCombined sources	1
Modified residueⁱ	636	N6-acetyllysineCombined sources	1
Modified residueⁱ	680	PhosphoserineCombined sources	1
Modified residueⁱ	840	PhosphothreonineCombined sources	1
Modified residueⁱ	926	PhosphoserineCombined sources	1
Modified residueⁱ	1056	PhosphoserineCombined sources	1
Modified residueⁱ	1130	N6-acetyllysineCombined sources	1
Modified residueⁱ	1235	N6-acetyllysineCombined sources	1
Modified residueⁱ	1837	PhosphoserineCombined sources	1
Modified residueⁱ	1845	PhosphothreonineCombined sources	1
Modified residueⁱ	1858	PhosphoserineCombined sources	1
Modified residueⁱ	2098	PhosphoserineCombined sources	1
Modified residueⁱ	2147	PhosphothreonineCombined sources	1
Modified residueⁱ	2151	PhosphoserineCombined sources	1
Modified residueⁱ	2201	PhosphoserineCombined sources	1
Modified residueⁱ	2525	PhosphothreonineCombined sources	1
Cross-linkⁱ	2528	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	2611	PhosphoserineCombined sources	1
Modified residueⁱ	2796	PhosphoserineCombined sources	1
Modified residueⁱ	2955	PhosphoserineCombined sources	1
Modified residueⁱ	2958	N6-acetyllysineBy similarity	1
Modified residueⁱ	3036	PhosphoserineCombined sources	1
Modified residueⁱ	3372	PhosphothreonineCombined sources	1
Modified residueⁱ	3462	N6-acetyllysineBy similarity	1
Modified residueⁱ	3511	PhosphoserineCombined sources	1
Modified residueⁱ	3515	PhosphoserineCombined sources	1
Modified residueⁱ	3527	PhosphoserineCombined sources	1

Post-translational modificationⁱ

Proteolytic cleavage by TASP1 generates MLL cleavage product N320 and MLL cleavage product C180, which reassemble through a non-covalent association. 2 cleavage sites exist, cleavage site 1 (CS1) and cleavage site 2 (CS2), to generate MLL cleavage products N320 and C180. CS2 is the major site.2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	2666 – 2667	Cleavage; by TASP1, site 11 Publication		2
Siteⁱ	2718 – 2719	Cleavage; by TASP1, site 21 Publication		2

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q03164
jPOSTⁱ	Q03164
MassIVEⁱ	Q03164
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q03164
PaxDbⁱ	Q03164
PeptideAtlas More...PeptideAtlasⁱ	Q03164
PRIDEⁱ	Q03164
ProteomicsDBⁱ	23014 58195 [Q03164-1] 58196 [Q03164-2]

PTM databases

CarbonylDBⁱ	Q03164
GlyConnectⁱ	2046
iPTMnetⁱ	Q03164
PhosphoSitePlusⁱ	Q03164

Expressionⁱ

Tissue specificityⁱ

Heart, lung, brain and T- and B-lymphocytes.

Gene expression databases

Bgeeⁱ	ENSG00000118058 Expressed in forebrain and 243 other tissues
ExpressionAtlasⁱ	Q03164 baseline and differential
Genevisibleⁱ	Q03164 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000118058 Low tissue specificity

HPAⁱ

ENSG00000118058 Low tissue specificity

Interactionⁱ

Subunit structureⁱ

MLL cleavage product N320 heterodimerizes with MLL cleavage product C180 (via SET and FYRC domains).

Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15199122, PubMed:15960975, PubMed:17500065, PubMed:19556245, PubMed:19187761, PubMed:26886794).

Interacts (via WIN motif) with WDR5; the interaction is direct (PubMed:19556245, PubMed:18829459, PubMed:22665483, PubMed:18840606). Interaction with WDR5 is required for stable interaction with ASH2L and RBBP5, and thereby also for optimal histone methyltransferase activity (PubMed:26886794).

Interacts with KAT8/MOF; the interaction is direct (PubMed:15960975).

Interacts with SBF1 and PPP1R15A (PubMed:9537414, PubMed:10490642).

Interacts with ZNF335 (PubMed:23178126).

Interacts with CLOCK and ARNTL/BMAL1 in a circadian manner (By similarity).

Interacts with PPIE; this results in decreased histone H3 methyltransferase activity (PubMed:20677832, PubMed:20541251).

Interacts with CREBBP (PubMed:16253272).

Interacts with the WRAD complex composed of WDR5, RBBP5, ASH2L and DPY30 (PubMed:22665483).

Interacts (via MBM motif) with MEN1 (PubMed:22936661, PubMed:22327296, PubMed:25305204).

Interacts (via IBM motifs) with PSIP1 (via IBD domain) with moderate affinity whereas the KMT2A-MEN1 complex interacts with a greater affinity; MEN1 enhances interaction of KMT2A with PSIP1 (PubMed:22327296, PubMed:25305204, PubMed:25082813, PubMed:29997176). Phosphorylation increases its affinity for PSIP1 (PubMed:29997176).

Forms a complex with CREBBP and CREB1 (PubMed:23651431).

By similarity24 Publications

Binary interactionsⁱ

Hide details

Q03164

With	#Exp.	IntAct
AR [P10275]	2	EBI-591370,EBI-608057
ASH2L - isoform 3 [Q9UBL3-3]	4	EBI-591370,EBI-16130425
CDC73 [Q6P1J9]	4	EBI-591370,EBI-930143
CTR9 [Q6PD62]	5	EBI-591370,EBI-1019583
H3C12 [P68431]	11	EBI-591370,EBI-79722
KAT8 [Q9H7Z6]	3	EBI-591370,EBI-896414
itself	5	EBI-591370,EBI-591370
MEN1 - isoform 2 [O00255-2]	12	EBI-591370,EBI-9869387
PAF1 [Q8N7H5]	4	EBI-591370,EBI-2607770
PPIE [Q9UNP9]	4	EBI-591370,EBI-591818
RBBP5 [Q15291]	9	EBI-591370,EBI-592823
SIRT1 [Q96EB6]	5	EBI-591370,EBI-1802965
SKP2 - isoform 1 [Q13309-1]	2	EBI-591370,EBI-15490084
WDR5 [P61964]	13	EBI-591370,EBI-540834
Arntl [Q9WTL8] from Mus musculus.	3	EBI-591370,EBI-644534
Clock [O08785] from Mus musculus.	3	EBI-591370,EBI-79859
Crebbp [P45481] from Mus musculus.	7	EBI-591370,EBI-296306

MLL cleavage product N320 (PRO_0000390949)

With	#Exp.	IntAct
PAX5 [Q02548]	2	EBI-2610266,EBI-296331

MLL cleavage product C180 (PRO_0000390950)

With	#Exp.	IntAct
KAT6A [Q92794]	10	EBI-2638616,EBI-948013
WDR5 [P61964]	2	EBI-2638616,EBI-540834

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	110443, 133 interactors
CORUMⁱ	Q03164
Database of interacting proteins More...DIPⁱ	DIP-29221N
ELMⁱ	Q03164
IntActⁱ	Q03164, 62 interactors
Molecular INTeraction database More...MINTⁱ	Q03164
STRINGⁱ	9606.ENSP00000436786

Chemistry databases

BindingDBⁱ	Q03164

BindingDBⁱ

Q03164

Miscellaneous databases

RNActⁱ	Q03164 protein

RNActⁱ

Q03164 protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	114 – 133	Combined sources	20
Beta strandⁱ	135 – 138	Combined sources	4
Beta strandⁱ	140 – 145	Combined sources	6
Beta strandⁱ	150 – 152	Combined sources	3
Beta strandⁱ	1151 – 1154	Combined sources	4
Beta strandⁱ	1156 – 1158	Combined sources	3
Helixⁱ	1159 – 1162	Combined sources	4
Beta strandⁱ	1168 – 1170	Combined sources	3
Helixⁱ	1171 – 1175	Combined sources	5
Helixⁱ	1177 – 1179	Combined sources	3
Beta strandⁱ	1183 – 1185	Combined sources	3
Turnⁱ	1190 – 1192	Combined sources	3
Beta strandⁱ	1197 – 1200	Combined sources	4
Turnⁱ	1204 – 1206	Combined sources	3
Beta strandⁱ	1566 – 1568	Combined sources	3
Turnⁱ	1570 – 1572	Combined sources	3
Beta strandⁱ	1575 – 1577	Combined sources	3
Turnⁱ	1578 – 1582	Combined sources	5
Beta strandⁱ	1585 – 1587	Combined sources	3
Turnⁱ	1589 – 1591	Combined sources	3
Beta strandⁱ	1594 – 1596	Combined sources	3
Helixⁱ	1597 – 1599	Combined sources	3
Helixⁱ	1604 – 1612	Combined sources	9
Helixⁱ	1614 – 1617	Combined sources	4
Turnⁱ	1622 – 1624	Combined sources	3
Beta strandⁱ	1627 – 1629	Combined sources	3
Helixⁱ	1631 – 1652	Combined sources	22
Helixⁱ	1655 – 1661	Combined sources	7
Helixⁱ	1708 – 1716	Combined sources	9
Helixⁱ	1723 – 1740	Combined sources	18
Helixⁱ	1745 – 1765	Combined sources	21
Helixⁱ	1771 – 1773	Combined sources	3
Helixⁱ	2847 – 2855	Combined sources	9
Helixⁱ	3764 – 3766	Combined sources	3
Helixⁱ	3796 – 3799	Combined sources	4
Helixⁱ	3809 – 3811	Combined sources	3
Helixⁱ	3816 – 3820	Combined sources	5
Helixⁱ	3823 – 3830	Combined sources	8
Beta strandⁱ	3831 – 3835	Combined sources	5
Beta strandⁱ	3837 – 3847	Combined sources	11
Beta strandⁱ	3854 – 3857	Combined sources	4
Beta strandⁱ	3860 – 3864	Combined sources	5
Helixⁱ	3865 – 3867	Combined sources	3
Helixⁱ	3868 – 3877	Combined sources	10
Beta strandⁱ	3884 – 3886	Combined sources	3
Beta strandⁱ	3888 – 3894	Combined sources	7
Turnⁱ	3896 – 3898	Combined sources	3
Helixⁱ	3901 – 3904	Combined sources	4
Beta strandⁱ	3912 – 3920	Combined sources	9
Beta strandⁱ	3923 – 3932	Combined sources	10
Beta strandⁱ	3939 – 3942	Combined sources	4

Show more details

3D structure databases

SMRⁱ	Q03164
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q03164

EvolutionaryTraceⁱ

Q03164

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	1703 – 1748	Bromo; divergentPROSITE-ProRule annotationAdd BLAST	46
Domainⁱ	2018 – 2074	FYR N-terminalPROSITE-ProRule annotationAdd BLAST	57
Domainⁱ	3666 – 3747	FYR C-terminalPROSITE-ProRule annotationAdd BLAST	82
Domainⁱ	3829 – 3945	SETPROSITE-ProRule annotationAdd BLAST	117
Domainⁱ	3953 – 3969	Post-SETPROSITE-ProRule annotationAdd BLAST	17

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	1584 – 1600	Interaction with histone H3K4me31 PublicationAdd BLAST		17
Regionⁱ	3906 – 3907	S-adenosyl-L-methionine bindingCombined sources2 Publications		2

Motif

Feature key	Position(s)	DescriptionActions	Length
Motifⁱ	6 – 25	Menin-binding motif (MBM)1 PublicationAdd BLAST	20
Motifⁱ	123 – 134	Integrase domain-binding motif 1 (IBM1)1 PublicationAdd BLAST	12
Motifⁱ	147 – 152	Integrase domain-binding motif 2 (IBM2)1 Publication	6
Motifⁱ	2847 – 2855	9aaTAD1 Publication	9
Motifⁱ	3762 – 3767	WDR5 interaction motif (WIN)2 Publications	6

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	17 – 102	Ala/Gly/Ser-richAdd BLAST	86
Compositional biasⁱ	137 – 143	Poly-Gly	7
Compositional biasⁱ	561 – 564	Poly-Pro	4
Compositional biasⁱ	568 – 571	Poly-Pro	4

Domainⁱ

The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

The SET domain structure is atypical and is not in an optimal position to have methyltransferase activity. It requires other components of the MLL1/MLL complex, such as ASH2L or RBBP5, to order the active site and obtain optimal histone methyltransferase activity.2 Publications

The CXXC-type zinc finger binds to DNA sequence elements containing unnmethylated CpG dinucleotides.3 Publications

The third PHD-type zinc-finger binds both trimethylated histone H3K4me3 and PPIE; histone and PPIE bind to distinct surfaces (PubMed:20677832, PubMed:20541251). Nevertheless, PPIE binding and histone binding are mutually inhibitory (PubMed:20677832). Isomerization of a peptidylproline bond in the linker between the third PHD-type zinc-finger and the bromo domain disrupts the interaction between the bromo domain and the third PHD-type zinc-finger, and thereby facilitates interaction with PPIE (PubMed:20541251).2 Publications

Sequence similaritiesⁱ

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation

Zinc finger

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	1147 – 1195	CXXC-typePROSITE-ProRule annotation1 PublicationAdd BLAST	49
Zinc fingerⁱ	1431 – 1482	PHD-type 1PROSITE-ProRule annotationAdd BLAST	52
Zinc fingerⁱ	1479 – 1533	PHD-type 2PROSITE-ProRule annotationAdd BLAST	55
Zinc fingerⁱ	1566 – 1627	PHD-type 3PROSITE-ProRule annotationAdd BLAST	62
Zinc fingerⁱ	1870 – 1910	C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST	41
Zinc fingerⁱ	1931 – 1978	PHD-type 4PROSITE-ProRule annotationAdd BLAST	48

Keywords - Domainⁱ

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG1084 Eukaryota COG2940 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000160099
HOGENOMⁱ	CLU_000208_2_0_1
InParanoidⁱ	Q03164
KEGG Orthology (KO) More...KOⁱ	K09186
OMAⁱ	YDSKMME
Database of Orthologous Groups More...OrthoDBⁱ	738155at2759
PhylomeDBⁱ	Q03164
TreeFamⁱ	TF319820

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd15693 ePHD_KMT2A, 1 hit cd15588 PHD1_KMT2A, 1 hit cd15590 PHD2_KMT2A, 1 hit
Database of protein disorder More...DisProtⁱ	DP01116
Gene3Dⁱ	3.30.40.10, 3 hits
IDEALⁱ	IID00379
InterProⁱ	View protein in InterPro IPR001487 Bromodomain IPR036427 Bromodomain-like_sf IPR034732 EPHD IPR003889 FYrich_C IPR003888 FYrich_N IPR037927 KMT2A IPR041958 KMT2A_ePHD IPR042023 KMT2A_PHD1 IPR042025 KMT2A_PHD2 IPR016569 MeTrfase_trithorax IPR003616 Post-SET_dom IPR001214 SET_dom IPR002857 Znf_CXXC IPR011011 Znf_FYVE_PHD IPR001965 Znf_PHD IPR019787 Znf_PHD-finger IPR013083 Znf_RING/FYVE/PHD
PANTHERⁱ	PTHR45838:SF2 PTHR45838:SF2, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF05965 FYRC, 1 hit PF05964 FYRN, 1 hit PF00628 PHD, 2 hits PF00856 SET, 1 hit PF02008 zf-CXXC, 1 hit
PIRSFⁱ	PIRSF010354 Methyltransferase_trithorax, 1 hit
SMARTⁱ	View protein in SMART SM00297 BROMO, 1 hit SM00542 FYRC, 1 hit SM00541 FYRN, 1 hit SM00249 PHD, 4 hits SM00508 PostSET, 1 hit SM00317 SET, 1 hit
SUPFAMⁱ	SSF47370 SSF47370, 1 hit SSF57903 SSF57903, 2 hits
PROSITEⁱ	View protein in PROSITE PS50014 BROMODOMAIN_2, 1 hit PS51805 EPHD, 1 hit PS51543 FYRC, 1 hit PS51542 FYRN, 1 hit PS50868 POST_SET, 1 hit PS50280 SET, 1 hit PS51058 ZF_CXXC, 1 hit PS01359 ZF_PHD_1, 3 hits PS50016 ZF_PHD_2, 3 hits

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 8 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q03164-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ 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
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG 
        60         70         80         90        100
PGAPPSPPAV AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS 
       110        120        130        140        150
SGPALLRVGP GFDAALQVSA AIGTNLRRFR AVFGESGGGG GSGEDEQFLG 
       160        170        180        190        200
FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR SGSDRNSAIL SDPSVFSPLN 
       210        220        230        240        250
KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD ISELPKGNKE 
       260        270        280        290        300
DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV 
       310        320        330        340        350
RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ 
       360        370        380        390        400
SPRRIKPVRI IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK 
       410        420        430        440        450
TQVKNIRQFI MPVVSAISSR IIKTPRRFIE DEDYDPPIKI ARLESTPNSR 
       460        470        480        490        500
FSAPSCGSSE KSSAASQHSS QMSSDSSRSS SPSVDTSTDS QASEEIQVLP 
       510        520        530        540        550
EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS RTTKKLSTLQ 
       560        570        580        590        600
SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS 
       610        620        630        640        650
TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN 
       660        670        680        690        700
FRPPPLTPED VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP 
       710        720        730        740        750
RFTPSEAHSR IFESVTLPSN RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS 
       760        770        780        790        800
PSHSMRTRSG RLSSSELSPL TPPSSVSSSL SISVSPLATS ALNPTFTFPS 
       810        820        830        840        850
HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT PGSQTERGRN 
       860        870        880        890        900
KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ 
       910        920        930        940        950
SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL 
       960        970        980        990       1000
GDTTAVKTKI LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK 
      1010       1020       1030       1040       1050
HSTSSIGSML AQADKLPMTD KRVASLLKKA KAQLCKIEKS KSLKQTDQPK 
      1060       1070       1080       1090       1100
AQGQESDSSE TSVRGPRIKH VCRRAAVALG RKRAVFPDDM PTLSALPWEE 
      1110       1120       1130       1140       1150
REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA PQEPPVKKGR 
      1160       1170       1180       1190       1200
RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM 
      1210       1220       1230       1240       1250
PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE 
      1260       1270       1280       1290       1300
DPAPKKSSSE PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ 
      1310       1320       1330       1340       1350
PALVIPPQPP TTGPPRKEVP KTTPSEPKKK QPPPPESGPE QSKQKKVAPR 
      1360       1370       1380       1390       1400
PSIPVKQKPK EKEKPPPVNK QENAGTLNIL STLSNGNSSK QKIPADGVHR 
      1410       1420       1430       1440       1450
IRVDFKEDCE AENVWEMGGL GILTSVPITP RVVCFLCASS GHVEFVYCQV 
      1460       1470       1480       1490       1500
CCEPFHKFCL EENERPLEDQ LENWCCRRCK FCHVCGRQHQ ATKQLLECNK 
      1510       1520       1530       1540       1550
CRNSYHPECL GPNYPTKPTK KKKVWICTKC VRCKSCGSTT PGKGWDAQWS 
      1560       1570       1580       1590       1600
HDFSLCHDCA KLFAKGNFCP LCDKCYDDDD YESKMMQCGK CDRWVHSKCE 
      1610       1620       1630       1640       1650
NLSDEMYEIL SNLPESVAYT CVNCTERHPA EWRLALEKEL QISLKQVLTA 
      1660       1670       1680       1690       1700
LLNSRTTSHL LRYRQAAKPP DLNPETEESI PSRSSPEGPD PPVLTEVSKQ 
      1710       1720       1730       1740       1750
DDQQPLDLEG VKRKMDQGNY TSVLEFSDDI VKIIQAAINS DGGQPEIKKA 
      1760       1770       1780       1790       1800
NSMVKSFFIR QMERVFPWFS VKKSRFWEPN KVSSNSGMLP NAVLPPSLDH 
      1810       1820       1830       1840       1850
NYAQWQEREE NSHTEQPPLM KKIIPAPKPK GPGEPDSPTP LHPPTPPILS 
      1860       1870       1880       1890       1900
TDRSREDSPE LNPPPGIEDN RQCALCLTYG DDSANDAGRL LYIGQNEWTH 
      1910       1920       1930       1940       1950
VNCALWSAEV FEDDDGSLKN VHMAVIRGKQ LRCEFCQKPG ATVGCCLTSC 
      1960       1970       1980       1990       2000
TSNYHFMCSR AKNCVFLDDK KVYCQRHRDL IKGEVVPENG FEVFRRVFVD 
      2010       2020       2030       2040       2050
FEGISLRRKF LNGLEPENIH MMIGSMTIDC LGILNDLSDC EDKLFPIGYQ 
      2060       2070       2080       2090       2100
CSRVYWSTTD ARKRCVYTCK IVECRPPVVE PDINSTVEHD ENRTIAHSPT 
      2110       2120       2130       2140       2150
SFTESSSKES QNTAEIISPP SPDRPPHSQT SGSCYYHVIS KVPRIRTPSY 
      2160       2170       2180       2190       2200
SPTQRSPGCR PLPSAGSPTP TTHEIVTVGD PLLSSGLRSI GSRRHSTSSL 
      2210       2220       2230       2240       2250
SPQRSKLRIM SPMRTGNTYS RNNVSSVSTT GTATDLESSA KVVDHVLGPL 
      2260       2270       2280       2290       2300
NSSTSLGQNT STSSNLQRTV VTVGNKNSHL DGSSSSEMKQ SSASDLVSKS 
      2310       2320       2330       2340       2350
SSLKGEKTKV LSSKSSEGSA HNVAYPGIPK LAPQVHNTTS RELNVSKIGS 
      2360       2370       2380       2390       2400
FAEPSSVSFS SKEALSFPHL HLRGQRNDRD QHTDSTQSAN SSPDEDTEVK 
      2410       2420       2430       2440       2450
TLKLSGMSNR SSIINEHMGS SSRDRRQKGK KSCKETFKEK HSSKSFLEPG 
      2460       2470       2480       2490       2500
QVTTGEEGNL KPEFMDEVLT PEYMGQRPCN NVSSDKIGDK GLSMPGVPKA 
      2510       2520       2530       2540       2550
PPMQVEGSAK ELQAPRKRTV KVTLTPLKME NESQSKNALK ESSPASPLQI 
      2560       2570       2580       2590       2600
ESTSPTEPIS ASENPGDGPV AQPSPNNTSC QDSQSNNYQN LPVQDRNLML 
      2610       2620       2630       2640       2650
PDGPKPQEDG SFKRRYPRRS ARARSNMFFG LTPLYGVRSY GEEDIPFYSS 
      2660       2670       2680       2690       2700
STGKKRGKRS AEGQVDGADD LSTSDEDDLY YYNFTRTVIS SGGEERLASH 
      2710       2720       2730       2740       2750
NLFREEEQCD LPKISQLDGV DDGTESDTSV TATTRKSSQI PKRNGKENGT 
      2760       2770       2780       2790       2800
ENLKIDRPED AGEKEHVTKS SVGHKNEPKM DNCHSVSRVK TQGQDSLEAQ 
      2810       2820       2830       2840       2850
LSSLESSRRV HTSTPSDKNL LDTYNTELLK SDSDNNNSDD CGNILPSDIM 
      2860       2870       2880       2890       2900
DFVLKNTPSM QALGESPESS SSELLNLGEG LGLDSNREKD MGLFEVFSQQ 
      2910       2920       2930       2940       2950
LPTTEPVDSS VSSSISAEEQ FELPLELPSD LSVLTTRSPT VPSQNPSRLA 
      2960       2970       2980       2990       3000
VISDSGEKRV TITEKSVASS ESDPALLSPG VDPTPEGHMT PDHFIQGHMD 
      3010       3020       3030       3040       3050
ADHISSPPCG SVEQGHGNNQ DLTRNSSTPG LQVPVSPTVP IQNQKYVPNS 
      3060       3070       3080       3090       3100
TDSPGPSQIS NAAVQTTPPH LKPATEKLIV VNQNMQPLYV LQTLPNGVTQ 
      3110       3120       3130       3140       3150
KIQLTSSVSS TPSVMETNTS VLGPMGGGLT LTTGLNPSLP TSQSLFPSAS 
      3160       3170       3180       3190       3200
KGLLPMSHHQ HLHSFPAATQ SSFPPNISNP PSGLLIGVQP PPDPQLLVSE 
      3210       3220       3230       3240       3250
SSQRTDLSTT VATPSSGLKK RPISRLQTRK NKKLAPSSTP SNIAPSDVVS 
      3260       3270       3280       3290       3300
NMTLINFTPS QLPNHPSLLD LGSLNTSSHR TVPNIIKRSK SSIMYFEPAP 
      3310       3320       3330       3340       3350
LLPQSVGGTA ATAAGTSTIS QDTSHLTSGS VSGLASSSSV LNVVSMQTTT 
      3360       3370       3380       3390       3400
TPTSSASVPG HVTLTNPRLL GTPDIGSISN LLIKASQQSL GIQDQPVALP 
      3410       3420       3430       3440       3450
PSSGMFPQLG TSQTPSTAAI TAASSICVLP STQTTGITAA SPSGEADEHY 
      3460       3470       3480       3490       3500
QLQHVNQLLA SKTGIHSSQR DLDSASGPQV SNFTQTVDAP NSMGLEQNKA 
      3510       3520       3530       3540       3550
LSSAVQASPT SPGGSPSSPS SGQRSASPSV PGPTKPKPKT KRFQLPLDKG 
      3560       3570       3580       3590       3600
NGKKHKVSHL RTSSSEAHIP DQETTSLTSG TGTPGAEAEQ QDTASVEQSS 
      3610       3620       3630       3640       3650
QKECGQPAGQ VAVLPEVQVT QNPANEQESA EPKTVEEEES NFSSPLMLWL 
      3660       3670       3680       3690       3700
QQEQKRKESI TEKKPKKGLV FEISSDDGFQ ICAESIEDAW KSLTDKVQEA 
      3710       3720       3730       3740       3750
RSNARLKQLS FAGVNGLRML GILHDAVVFL IEQLSGAKHC RNYKFRFHKP 
      3760       3770       3780       3790       3800
EEANEPPLNP HGSARAEVHL RKSAFDMFNF LASKHRQPPE YNPNDEEEEE 
      3810       3820       3830       3840       3850
VQLKSARRAT SMDLPMPMRF RHLKKTSKEA VGVYRSPIHG RGLFCKRNID 
      3860       3870       3880       3890       3900
AGEMVIEYAG NVIRSIQTDK REKYYDSKGI GCYMFRIDDS EVVDATMHGN 
      3910       3920       3930       3940       3950
AARFINHSCE PNCYSRVINI DGQKHIVIFA MRKIYRGEEL TYDYKFPIED 
      3960 
ASNKLPCNCG AKKCRKFLN

Length:3,969

Mass (Da):431,764

Last modified:May 1, 2007 - v5

Checksum:ⁱ1150F37EAB1430D3

Isoform 2 (identifier: Q03164-2) [UniParc]FASTA Add to basket

Also known as: 14P-18B

The sequence of this isoform differs from the canonical sequence as follows:
1407-1444: Missing.

« Hide

        10         20         30         40         50
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG 
        60         70         80         90        100
PGAPPSPPAV AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS 
       110        120        130        140        150
SGPALLRVGP GFDAALQVSA AIGTNLRRFR AVFGESGGGG GSGEDEQFLG 
       160        170        180        190        200
FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR SGSDRNSAIL SDPSVFSPLN 
       210        220        230        240        250
KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD ISELPKGNKE 
       260        270        280        290        300
DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV 
       310        320        330        340        350
RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ 
       360        370        380        390        400
SPRRIKPVRI IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK 
       410        420        430        440        450
TQVKNIRQFI MPVVSAISSR IIKTPRRFIE DEDYDPPIKI ARLESTPNSR 
       460        470        480        490        500
FSAPSCGSSE KSSAASQHSS QMSSDSSRSS SPSVDTSTDS QASEEIQVLP 
       510        520        530        540        550
EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS RTTKKLSTLQ 
       560        570        580        590        600
SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS 
       610        620        630        640        650
TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN 
       660        670        680        690        700
FRPPPLTPED VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP 
       710        720        730        740        750
RFTPSEAHSR IFESVTLPSN RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS 
       760        770        780        790        800
PSHSMRTRSG RLSSSELSPL TPPSSVSSSL SISVSPLATS ALNPTFTFPS 
       810        820        830        840        850
HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT PGSQTERGRN 
       860        870        880        890        900
KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ 
       910        920        930        940        950
SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL 
       960        970        980        990       1000
GDTTAVKTKI LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK 
      1010       1020       1030       1040       1050
HSTSSIGSML AQADKLPMTD KRVASLLKKA KAQLCKIEKS KSLKQTDQPK 
      1060       1070       1080       1090       1100
AQGQESDSSE TSVRGPRIKH VCRRAAVALG RKRAVFPDDM PTLSALPWEE 
      1110       1120       1130       1140       1150
REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA PQEPPVKKGR 
      1160       1170       1180       1190       1200
RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM 
      1210       1220       1230       1240       1250
PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE 
      1260       1270       1280       1290       1300
DPAPKKSSSE PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ 
      1310       1320       1330       1340       1350
PALVIPPQPP TTGPPRKEVP KTTPSEPKKK QPPPPESGPE QSKQKKVAPR 
      1360       1370       1380       1390       1400
PSIPVKQKPK EKEKPPPVNK QENAGTLNIL STLSNGNSSK QKIPADGVHR 
      1410       1420       1430       1440       1450
IRVDFKFVYC QVCCEPFHKF CLEENERPLE DQLENWCCRR CKFCHVCGRQ 
      1460       1470       1480       1490       1500
HQATKQLLEC NKCRNSYHPE CLGPNYPTKP TKKKKVWICT KCVRCKSCGS 
      1510       1520       1530       1540       1550
TTPGKGWDAQ WSHDFSLCHD CAKLFAKGNF CPLCDKCYDD DDYESKMMQC 
      1560       1570       1580       1590       1600
GKCDRWVHSK CENLSDEMYE ILSNLPESVA YTCVNCTERH PAEWRLALEK 
      1610       1620       1630       1640       1650
ELQISLKQVL TALLNSRTTS HLLRYRQAAK PPDLNPETEE SIPSRSSPEG 
      1660       1670       1680       1690       1700
PDPPVLTEVS KQDDQQPLDL EGVKRKMDQG NYTSVLEFSD DIVKIIQAAI 
      1710       1720       1730       1740       1750
NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSSNSGM 
      1760       1770       1780       1790       1800
LPNAVLPPSL DHNYAQWQER EENSHTEQPP LMKKIIPAPK PKGPGEPDSP 
      1810       1820       1830       1840       1850
TPLHPPTPPI LSTDRSREDS PELNPPPGIE DNRQCALCLT YGDDSANDAG 
      1860       1870       1880       1890       1900
RLLYIGQNEW THVNCALWSA EVFEDDDGSL KNVHMAVIRG KQLRCEFCQK 
      1910       1920       1930       1940       1950
PGATVGCCLT SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR DLIKGEVVPE 
      1960       1970       1980       1990       2000
NGFEVFRRVF VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS 
      2010       2020       2030       2040       2050
DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIVECRPPV VEPDINSTVE 
      2060       2070       2080       2090       2100
HDENRTIAHS PTSFTESSSK ESQNTAEIIS PPSPDRPPHS QTSGSCYYHV 
      2110       2120       2130       2140       2150
ISKVPRIRTP SYSPTQRSPG CRPLPSAGSP TPTTHEIVTV GDPLLSSGLR 
      2160       2170       2180       2190       2200
SIGSRRHSTS SLSPQRSKLR IMSPMRTGNT YSRNNVSSVS TTGTATDLES 
      2210       2220       2230       2240       2250
SAKVVDHVLG PLNSSTSLGQ NTSTSSNLQR TVVTVGNKNS HLDGSSSSEM 
      2260       2270       2280       2290       2300
KQSSASDLVS KSSSLKGEKT KVLSSKSSEG SAHNVAYPGI PKLAPQVHNT 
      2310       2320       2330       2340       2350
TSRELNVSKI GSFAEPSSVS FSSKEALSFP HLHLRGQRND RDQHTDSTQS 
      2360       2370       2380       2390       2400
ANSSPDEDTE VKTLKLSGMS NRSSIINEHM GSSSRDRRQK GKKSCKETFK 
      2410       2420       2430       2440       2450
EKHSSKSFLE PGQVTTGEEG NLKPEFMDEV LTPEYMGQRP CNNVSSDKIG 
      2460       2470       2480       2490       2500
DKGLSMPGVP KAPPMQVEGS AKELQAPRKR TVKVTLTPLK MENESQSKNA 
      2510       2520       2530       2540       2550
LKESSPASPL QIESTSPTEP ISASENPGDG PVAQPSPNNT SCQDSQSNNY 
      2560       2570       2580       2590       2600
QNLPVQDRNL MLPDGPKPQE DGSFKRRYPR RSARARSNMF FGLTPLYGVR 
      2610       2620       2630       2640       2650
SYGEEDIPFY SSSTGKKRGK RSAEGQVDGA DDLSTSDEDD LYYYNFTRTV 
      2660       2670       2680       2690       2700
ISSGGEERLA SHNLFREEEQ CDLPKISQLD GVDDGTESDT SVTATTRKSS 
      2710       2720       2730       2740       2750
QIPKRNGKEN GTENLKIDRP EDAGEKEHVT KSSVGHKNEP KMDNCHSVSR 
      2760       2770       2780       2790       2800
VKTQGQDSLE AQLSSLESSR RVHTSTPSDK NLLDTYNTEL LKSDSDNNNS 
      2810       2820       2830       2840       2850
DDCGNILPSD IMDFVLKNTP SMQALGESPE SSSSELLNLG EGLGLDSNRE 
      2860       2870       2880       2890       2900
KDMGLFEVFS QQLPTTEPVD SSVSSSISAE EQFELPLELP SDLSVLTTRS 
      2910       2920       2930       2940       2950
PTVPSQNPSR LAVISDSGEK RVTITEKSVA SSESDPALLS PGVDPTPEGH 
      2960       2970       2980       2990       3000
MTPDHFIQGH MDADHISSPP CGSVEQGHGN NQDLTRNSST PGLQVPVSPT 
      3010       3020       3030       3040       3050
VPIQNQKYVP NSTDSPGPSQ ISNAAVQTTP PHLKPATEKL IVVNQNMQPL 
      3060       3070       3080       3090       3100
YVLQTLPNGV TQKIQLTSSV SSTPSVMETN TSVLGPMGGG LTLTTGLNPS 
      3110       3120       3130       3140       3150
LPTSQSLFPS ASKGLLPMSH HQHLHSFPAA TQSSFPPNIS NPPSGLLIGV 
      3160       3170       3180       3190       3200
QPPPDPQLLV SESSQRTDLS TTVATPSSGL KKRPISRLQT RKNKKLAPSS 
      3210       3220       3230       3240       3250
TPSNIAPSDV VSNMTLINFT PSQLPNHPSL LDLGSLNTSS HRTVPNIIKR 
      3260       3270       3280       3290       3300
SKSSIMYFEP APLLPQSVGG TAATAAGTST ISQDTSHLTS GSVSGLASSS 
      3310       3320       3330       3340       3350
SVLNVVSMQT TTTPTSSASV PGHVTLTNPR LLGTPDIGSI SNLLIKASQQ 
      3360       3370       3380       3390       3400
SLGIQDQPVA LPPSSGMFPQ LGTSQTPSTA AITAASSICV LPSTQTTGIT 
      3410       3420       3430       3440       3450
AASPSGEADE HYQLQHVNQL LASKTGIHSS QRDLDSASGP QVSNFTQTVD 
      3460       3470       3480       3490       3500
APNSMGLEQN KALSSAVQAS PTSPGGSPSS PSSGQRSASP SVPGPTKPKP 
      3510       3520       3530       3540       3550
KTKRFQLPLD KGNGKKHKVS HLRTSSSEAH IPDQETTSLT SGTGTPGAEA 
      3560       3570       3580       3590       3600
EQQDTASVEQ SSQKECGQPA GQVAVLPEVQ VTQNPANEQE SAEPKTVEEE 
      3610       3620       3630       3640       3650
ESNFSSPLML WLQQEQKRKE SITEKKPKKG LVFEISSDDG FQICAESIED 
      3660       3670       3680       3690       3700
AWKSLTDKVQ EARSNARLKQ LSFAGVNGLR MLGILHDAVV FLIEQLSGAK 
      3710       3720       3730       3740       3750
HCRNYKFRFH KPEEANEPPL NPHGSARAEV HLRKSAFDMF NFLASKHRQP 
      3760       3770       3780       3790       3800
PEYNPNDEEE EEVQLKSARR ATSMDLPMPM RFRHLKKTSK EAVGVYRSPI 
      3810       3820       3830       3840       3850
HGRGLFCKRN IDAGEMVIEY AGNVIRSIQT DKREKYYDSK GIGCYMFRID 
      3860       3870       3880       3890       3900
DSEVVDATMH GNAARFINHS CEPNCYSRVI NIDGQKHIVI FAMRKIYRGE 
      3910       3920       3930 
ELTYDYKFPI EDASNKLPCN CGAKKCRKFL N

Show »

Length:3,931

Mass (Da):427,733

Checksum:ⁱB8E736C88E83D50B

Isoform 3 (identifier: Q03164-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1603-1603: S → SGTE

« Hide

        10         20         30         40         50
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG 
        60         70         80         90        100
PGAPPSPPAV AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS 
       110        120        130        140        150
SGPALLRVGP GFDAALQVSA AIGTNLRRFR AVFGESGGGG GSGEDEQFLG 
       160        170        180        190        200
FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR SGSDRNSAIL SDPSVFSPLN 
       210        220        230        240        250
KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD ISELPKGNKE 
       260        270        280        290        300
DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV 
       310        320        330        340        350
RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ 
       360        370        380        390        400
SPRRIKPVRI IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK 
       410        420        430        440        450
TQVKNIRQFI MPVVSAISSR IIKTPRRFIE DEDYDPPIKI ARLESTPNSR 
       460        470        480        490        500
FSAPSCGSSE KSSAASQHSS QMSSDSSRSS SPSVDTSTDS QASEEIQVLP 
       510        520        530        540        550
EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS RTTKKLSTLQ 
       560        570        580        590        600
SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS 
       610        620        630        640        650
TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN 
       660        670        680        690        700
FRPPPLTPED VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP 
       710        720        730        740        750
RFTPSEAHSR IFESVTLPSN RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS 
       760        770        780        790        800
PSHSMRTRSG RLSSSELSPL TPPSSVSSSL SISVSPLATS ALNPTFTFPS 
       810        820        830        840        850
HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT PGSQTERGRN 
       860        870        880        890        900
KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ 
       910        920        930        940        950
SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL 
       960        970        980        990       1000
GDTTAVKTKI LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK 
      1010       1020       1030       1040       1050
HSTSSIGSML AQADKLPMTD KRVASLLKKA KAQLCKIEKS KSLKQTDQPK 
      1060       1070       1080       1090       1100
AQGQESDSSE TSVRGPRIKH VCRRAAVALG RKRAVFPDDM PTLSALPWEE 
      1110       1120       1130       1140       1150
REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA PQEPPVKKGR 
      1160       1170       1180       1190       1200
RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM 
      1210       1220       1230       1240       1250
PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE 
      1260       1270       1280       1290       1300
DPAPKKSSSE PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ 
      1310       1320       1330       1340       1350
PALVIPPQPP TTGPPRKEVP KTTPSEPKKK QPPPPESGPE QSKQKKVAPR 
      1360       1370       1380       1390       1400
PSIPVKQKPK EKEKPPPVNK QENAGTLNIL STLSNGNSSK QKIPADGVHR 
      1410       1420       1430       1440       1450
IRVDFKEDCE AENVWEMGGL GILTSVPITP RVVCFLCASS GHVEFVYCQV 
      1460       1470       1480       1490       1500
CCEPFHKFCL EENERPLEDQ LENWCCRRCK FCHVCGRQHQ ATKQLLECNK 
      1510       1520       1530       1540       1550
CRNSYHPECL GPNYPTKPTK KKKVWICTKC VRCKSCGSTT PGKGWDAQWS 
      1560       1570       1580       1590       1600
HDFSLCHDCA KLFAKGNFCP LCDKCYDDDD YESKMMQCGK CDRWVHSKCE 
      1610       1620       1630       1640       1650
NLSGTEDEMY EILSNLPESV AYTCVNCTER HPAEWRLALE KELQISLKQV 
      1660       1670       1680       1690       1700
LTALLNSRTT SHLLRYRQAA KPPDLNPETE ESIPSRSSPE GPDPPVLTEV 
      1710       1720       1730       1740       1750
SKQDDQQPLD LEGVKRKMDQ GNYTSVLEFS DDIVKIIQAA INSDGGQPEI 
      1760       1770       1780       1790       1800
KKANSMVKSF FIRQMERVFP WFSVKKSRFW EPNKVSSNSG MLPNAVLPPS 
      1810       1820       1830       1840       1850
LDHNYAQWQE REENSHTEQP PLMKKIIPAP KPKGPGEPDS PTPLHPPTPP 
      1860       1870       1880       1890       1900
ILSTDRSRED SPELNPPPGI EDNRQCALCL TYGDDSANDA GRLLYIGQNE 
      1910       1920       1930       1940       1950
WTHVNCALWS AEVFEDDDGS LKNVHMAVIR GKQLRCEFCQ KPGATVGCCL 
      1960       1970       1980       1990       2000
TSCTSNYHFM CSRAKNCVFL DDKKVYCQRH RDLIKGEVVP ENGFEVFRRV 
      2010       2020       2030       2040       2050
FVDFEGISLR RKFLNGLEPE NIHMMIGSMT IDCLGILNDL SDCEDKLFPI 
      2060       2070       2080       2090       2100
GYQCSRVYWS TTDARKRCVY TCKIVECRPP VVEPDINSTV EHDENRTIAH 
      2110       2120       2130       2140       2150
SPTSFTESSS KESQNTAEII SPPSPDRPPH SQTSGSCYYH VISKVPRIRT 
      2160       2170       2180       2190       2200
PSYSPTQRSP GCRPLPSAGS PTPTTHEIVT VGDPLLSSGL RSIGSRRHST 
      2210       2220       2230       2240       2250
SSLSPQRSKL RIMSPMRTGN TYSRNNVSSV STTGTATDLE SSAKVVDHVL 
      2260       2270       2280       2290       2300
GPLNSSTSLG QNTSTSSNLQ RTVVTVGNKN SHLDGSSSSE MKQSSASDLV 
      2310       2320       2330       2340       2350
SKSSSLKGEK TKVLSSKSSE GSAHNVAYPG IPKLAPQVHN TTSRELNVSK 
      2360       2370       2380       2390       2400
IGSFAEPSSV SFSSKEALSF PHLHLRGQRN DRDQHTDSTQ SANSSPDEDT 
      2410       2420       2430       2440       2450
EVKTLKLSGM SNRSSIINEH MGSSSRDRRQ KGKKSCKETF KEKHSSKSFL 
      2460       2470       2480       2490       2500
EPGQVTTGEE GNLKPEFMDE VLTPEYMGQR PCNNVSSDKI GDKGLSMPGV 
      2510       2520       2530       2540       2550
PKAPPMQVEG SAKELQAPRK RTVKVTLTPL KMENESQSKN ALKESSPASP 
      2560       2570       2580       2590       2600
LQIESTSPTE PISASENPGD GPVAQPSPNN TSCQDSQSNN YQNLPVQDRN 
      2610       2620       2630       2640       2650
LMLPDGPKPQ EDGSFKRRYP RRSARARSNM FFGLTPLYGV RSYGEEDIPF 
      2660       2670       2680       2690       2700
YSSSTGKKRG KRSAEGQVDG ADDLSTSDED DLYYYNFTRT VISSGGEERL 
      2710       2720       2730       2740       2750
ASHNLFREEE QCDLPKISQL DGVDDGTESD TSVTATTRKS SQIPKRNGKE 
      2760       2770       2780       2790       2800
NGTENLKIDR PEDAGEKEHV TKSSVGHKNE PKMDNCHSVS RVKTQGQDSL 
      2810       2820       2830       2840       2850
EAQLSSLESS RRVHTSTPSD KNLLDTYNTE LLKSDSDNNN SDDCGNILPS 
      2860       2870       2880       2890       2900
DIMDFVLKNT PSMQALGESP ESSSSELLNL GEGLGLDSNR EKDMGLFEVF 
      2910       2920       2930       2940       2950
SQQLPTTEPV DSSVSSSISA EEQFELPLEL PSDLSVLTTR SPTVPSQNPS 
      2960       2970       2980       2990       3000
RLAVISDSGE KRVTITEKSV ASSESDPALL SPGVDPTPEG HMTPDHFIQG 
      3010       3020       3030       3040       3050
HMDADHISSP PCGSVEQGHG NNQDLTRNSS TPGLQVPVSP TVPIQNQKYV 
      3060       3070       3080       3090       3100
PNSTDSPGPS QISNAAVQTT PPHLKPATEK LIVVNQNMQP LYVLQTLPNG 
      3110       3120       3130       3140       3150
VTQKIQLTSS VSSTPSVMET NTSVLGPMGG GLTLTTGLNP SLPTSQSLFP 
      3160       3170       3180       3190       3200
SASKGLLPMS HHQHLHSFPA ATQSSFPPNI SNPPSGLLIG VQPPPDPQLL 
      3210       3220       3230       3240       3250
VSESSQRTDL STTVATPSSG LKKRPISRLQ TRKNKKLAPS STPSNIAPSD 
      3260       3270       3280       3290       3300
VVSNMTLINF TPSQLPNHPS LLDLGSLNTS SHRTVPNIIK RSKSSIMYFE 
      3310       3320       3330       3340       3350
PAPLLPQSVG GTAATAAGTS TISQDTSHLT SGSVSGLASS SSVLNVVSMQ 
      3360       3370       3380       3390       3400
TTTTPTSSAS VPGHVTLTNP RLLGTPDIGS ISNLLIKASQ QSLGIQDQPV 
      3410       3420       3430       3440       3450
ALPPSSGMFP QLGTSQTPST AAITAASSIC VLPSTQTTGI TAASPSGEAD 
      3460       3470       3480       3490       3500
EHYQLQHVNQ LLASKTGIHS SQRDLDSASG PQVSNFTQTV DAPNSMGLEQ 
      3510       3520       3530       3540       3550
NKALSSAVQA SPTSPGGSPS SPSSGQRSAS PSVPGPTKPK PKTKRFQLPL 
      3560       3570       3580       3590       3600
DKGNGKKHKV SHLRTSSSEA HIPDQETTSL TSGTGTPGAE AEQQDTASVE 
      3610       3620       3630       3640       3650
QSSQKECGQP AGQVAVLPEV QVTQNPANEQ ESAEPKTVEE EESNFSSPLM 
      3660       3670       3680       3690       3700
LWLQQEQKRK ESITEKKPKK GLVFEISSDD GFQICAESIE DAWKSLTDKV 
      3710       3720       3730       3740       3750
QEARSNARLK QLSFAGVNGL RMLGILHDAV VFLIEQLSGA KHCRNYKFRF 
      3760       3770       3780       3790       3800
HKPEEANEPP LNPHGSARAE VHLRKSAFDM FNFLASKHRQ PPEYNPNDEE 
      3810       3820       3830       3840       3850
EEEVQLKSAR RATSMDLPMP MRFRHLKKTS KEAVGVYRSP IHGRGLFCKR 
      3860       3870       3880       3890       3900
NIDAGEMVIE YAGNVIRSIQ TDKREKYYDS KGIGCYMFRI DDSEVVDATM 
      3910       3920       3930       3940       3950
HGNAARFINH SCEPNCYSRV INIDGQKHIV IFAMRKIYRG EELTYDYKFP 
      3960       3970 
IEDASNKLPC NCGAKKCRKF LN

Show »

Length:3,972

Mass (Da):432,052

Checksum:ⁱ18CFDD8B9A763204

Computationally mapped potential isoform sequencesⁱ

There are 8 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E9PR05	E9PR05_HUMAN	Histone-lysine N-methyltransferase ... Histone-lysine N-methyltransferase 2A	KMT2A	1,439	Annotation score:
H7C5W4	H7C5W4_HUMAN	Histone-lysine N-methyltransferase ... Histone-lysine N-methyltransferase 2A	KMT2A	302	Annotation score:
H0YEU4	H0YEU4_HUMAN	Histone-lysine N-methyltransferase ... Histone-lysine N-methyltransferase 2A	KMT2A	87	Annotation score:
A0A3B3ISN4	A0A3B3ISN4_HUMAN	Histone-lysine N-methyltransferase ... Histone-lysine N-methyltransferase 2A	KMT2A	173	Annotation score:
A0A3B3ITZ6	A0A3B3ITZ6_HUMAN	Histone-lysine N-methyltransferase ... Histone-lysine N-methyltransferase 2A	KMT2A	237	Annotation score:
A0A3B3ITT7	A0A3B3ITT7_HUMAN	Histone-lysine N-methyltransferase ... Histone-lysine N-methyltransferase 2A	KMT2A	69	Annotation score:
H7C5V8	H7C5V8_HUMAN	Histone-lysine N-methyltransferase ... Histone-lysine N-methyltransferase 2A	KMT2A	160	Annotation score:
A0A3B3ITT0	A0A3B3ITT0_HUMAN	Histone-lysine N-methyltransferase ... Histone-lysine N-methyltransferase 2A	KMT2A	50	Annotation score:

Sequence cautionⁱ

The sequence AAA58669 differs from that shown. Reason: Frameshift.Curated

The sequence AAG26332 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

The sequence BAD92745 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	144	E → ELTTQIPCSWRTKGHIHDKK TEPFRLLAWSWCLN in CAA93625 (PubMed:8703835).Curated	1
Sequence conflictⁱ	556	Q → E in CAA93625 (PubMed:8703835).Curated	1
Sequence conflictⁱ	556	Q → E in L04731 (PubMed:1423625).Curated	1
Sequence conflictⁱ	1347	V → A in AAG26335 (PubMed:10706619).Curated	1
Sequence conflictⁱ	1487	R → G in AAA18644 (PubMed:8162575).Curated	1
Sequence conflictⁱ	1490	Q → R in AAG26335 (PubMed:10706619).Curated	1
Sequence conflictⁱ	1507	P → L in AAG26335 (PubMed:10706619).Curated	1
Sequence conflictⁱ	1513	N → T in AAG26335 (PubMed:10706619).Curated	1
Sequence conflictⁱ	1600	E → G in AAG26335 (PubMed:10706619).Curated	1
Sequence conflictⁱ	1616	S → C in AAB34770 (PubMed:7598802).Curated	1
Sequence conflictⁱ	1937	Q → H in AAA92511 (PubMed:1303259).Curated	1
Sequence conflictⁱ	2181	P → S in AAA92511 (PubMed:1303259).Curated	1
Sequence conflictⁱ	3556	K → N in L04731 (PubMed:1423625).Curated	1
Sequence conflictⁱ	3718	R → G in CAA93625 (PubMed:8703835).Curated	1
Sequence conflictⁱ	3759	N → D in CAA93625 (PubMed:8703835).Curated	1
Sequence conflictⁱ	3813	D → G in CAA93625 (PubMed:8703835).Curated	1
Sequence conflictⁱ	3901	A → R in AAA58669 (PubMed:1423624).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_021317	30	A → G1 PublicationCorresponds to variant dbSNP:rs9332745EnsemblClinVar.	1
Natural variantⁱVAR_021318	53	A → V1 PublicationCorresponds to variant dbSNP:rs9332747EnsemblClinVar.	1
Natural variantⁱVAR_021319	502	E → K1 PublicationCorresponds to variant dbSNP:rs9332772EnsemblClinVar.	1
Natural variantⁱVAR_052652	1975	Q → P. Corresponds to variant dbSNP:rs693598Ensembl.	1
Natural variantⁱVAR_021320	2319	S → T1 PublicationCorresponds to variant dbSNP:rs9332837Ensembl.	1
Natural variantⁱVAR_021321	2354	P → R1 Publication

Annotation systems

Supporting data

UniProtKB - Q03164 (KMT2A_HUMAN)

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Histone-lysine N-methyltransferase 2A

KMT2A

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Nucleus

Nucleus

Cytosol

Nucleus

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Sites

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Motif

Compositional bias

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ