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Protein

Histone-lysine N-methyltransferase 2A

Gene

Kmt2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. 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'. Required for transcriptional activation of HOXA9. Promotes PPP1R15A-induced apoptosis (By similarity). 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 (PubMed:21113167).By similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei2662 – 26632Cleavage; by TASP1, site 1By similarity
Sitei2714 – 27152Cleavage; by TASP1, site 2By similarity
Sitei3762 – 37621Important for WDR5-recognition and bindingBy similarity
Binding sitei3836 – 38361S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei3838 – 38381S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei3880 – 38801S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi3906 – 39061ZincBy similarity
Metal bindingi3954 – 39541ZincBy similarity
Binding sitei3955 – 39551S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi3956 – 39561ZincBy similarity
Metal bindingi3961 – 39611ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi167 – 17812A.T hook 1Add
BLAST
DNA bindingi215 – 22511A.T hook 2Add
BLAST
DNA bindingi299 – 3079A.T hook 3
Zinc fingeri1144 – 119249CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1430 – 148152PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1478 – 153255PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1565 – 162965PHD-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. core promoter sequence-specific DNA binding Source: UniProtKB
  3. histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
  4. identical protein binding Source: MGI
  5. lysine-acetylated histone binding Source: UniProtKB
  6. protein homodimerization activity Source: MGI
  7. transcription regulatory region DNA binding Source: MGI
  8. unmethylated CpG binding Source: UniProtKB
  9. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. anterior/posterior pattern specification Source: MGI
  2. circadian regulation of gene expression Source: UniProtKB
  3. DNA methylation Source: MGI
  4. embryonic hemopoiesis Source: MGI
  5. histone H3-K4 methylation Source: UniProtKB
  6. histone H3-K4 trimethylation Source: MGI
  7. histone H4-K16 acetylation Source: UniProtKB
  8. negative regulation of cell proliferation Source: MGI
  9. positive regulation of cellular response to drug Source: MGI
  10. positive regulation of histone H3-K4 methylation Source: UniProtKB
  11. positive regulation of transcription, DNA-templated Source: UniProtKB
  12. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  13. positive regulation of transporter activity Source: MGI
  14. protein complex assembly Source: MGI
  15. regulation of histone H3-K14 acetylation Source: UniProtKB
  16. regulation of histone H3-K4 methylation Source: MGI
  17. regulation of histone H3-K9 acetylation Source: UniProtKB
  18. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase 2A (EC:2.1.1.43)
Short name:
Lysine N-methyltransferase 2A
Alternative name(s):
ALL-1
Myeloid/lymphoid or mixed-lineage leukemia
Myeloid/lymphoid or mixed-lineage leukemia protein 1
Zinc finger protein HRX
Cleaved into the following 2 chains:
Alternative name(s):
N-terminal cleavage product of 320 kDa
Short name:
p320
Alternative name(s):
C-terminal cleavage product of 180 kDa
Short name:
p180
Gene namesi
Name:Kmt2a
Synonyms:All1, Hrx, Mll, Mll1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:96995. Kmt2a.

Subcellular locationi

Nucleus By similarity
Chain MLL cleavage product C180 : Nucleus By similarity
Note: Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. histone methyltransferase complex Source: UniProtKB
  3. MLL1 complex Source: UniProtKB
  4. nucleoplasm Source: MGI
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 39663966Histone-lysine N-methyltransferase 2APRO_0000124877Add
BLAST
Chaini1 – 27142714MLL cleavage product N320By similarityPRO_0000390951Add
BLAST
Chaini2715 – 39661252MLL cleavage product C180By similarityPRO_0000390952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei151 – 1511PhosphoserineBy similarity
Modified residuei195 – 1951PhosphoserineBy similarity
Cross-linki214 – 214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki218 – 218Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki219 – 219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei237 – 2371N6-acetyllysine1 Publication
Modified residuei371 – 3711N6-acetyllysine1 Publication
Modified residuei516 – 5161PhosphoserineBy similarity
Modified residuei634 – 6341N6-acetyllysineBy similarity
Modified residuei678 – 6781PhosphoserineBy similarity
Modified residuei837 – 8371PhosphothreonineBy similarity
Modified residuei923 – 9231PhosphoserineBy similarity
Modified residuei1053 – 10531PhosphoserineBy similarity
Modified residuei1127 – 11271N6-acetyllysineBy similarity
Modified residuei1232 – 12321N6-acetyllysineBy similarity
Modified residuei1839 – 18391PhosphoserineBy similarity
Modified residuei1847 – 18471PhosphothreonineBy similarity
Modified residuei1860 – 18601PhosphoserineBy similarity
Modified residuei2100 – 21001PhosphoserineBy similarity
Modified residuei2148 – 21481PhosphothreonineBy similarity
Modified residuei2152 – 21521PhosphoserineBy similarity
Modified residuei2202 – 22021PhosphoserineBy similarity
Modified residuei2951 – 29511PhosphoserineBy similarity
Modified residuei2954 – 29541N6-acetyllysine1 Publication
Modified residuei3032 – 30321PhosphoserineBy similarity
Modified residuei3369 – 33691PhosphothreonineBy similarity
Modified residuei3459 – 34591N6-acetyllysine1 Publication
Modified residuei3510 – 35101PhosphoserineBy similarity

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.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP55200.
PaxDbiP55200.
PRIDEiP55200.

PTM databases

PhosphoSiteiP55200.

Expressioni

Gene expression databases

BgeeiP55200.
CleanExiMM_MLL1.
ExpressionAtlasiP55200. baseline and differential.
GenevestigatoriP55200.

Interactioni

Subunit structurei

MLL cleavage product N320 heterodimerizes with MLL cleavage product C180 (via SET and FYRC domains). Interacts with WDR5; the interaction is direct. Interacts with KAT8/MOF; the interaction is direct. Interacts with SBF1 and PPP1R15A (By similarity). Interacts with ZNF335 (By similarity). Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCF1/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. Interacts with CLOCK and ARNTL/BMAL1 in a circadian manner.By similarity2 Publications

Protein-protein interaction databases

DIPiDIP-58597N.
IntActiP55200. 1 interaction.
MINTiMINT-4084570.

Structurei

3D structure databases

ProteinModelPortaliP55200.
SMRiP55200. Positions 6-39, 101-133, 1147-1197, 1563-1781, 2836-2865, 3787-3966.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1705 – 175046Bromo; divergentPROSITE-ProRule annotationAdd
BLAST
Domaini2020 – 207657FYR N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini3663 – 374482FYR C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini3826 – 3942117SETPROSITE-ProRule annotationAdd
BLAST
Domaini3950 – 396617Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3903 – 39042S-adenosyl-L-methionine bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi14 – 150137Gly-richAdd
BLAST
Compositional biasi17 – 10084Ala/Gly/Ser-richAdd
BLAST
Compositional biasi80 – 9920Ser-richAdd
BLAST
Compositional biasi135 – 1417Poly-Gly
Compositional biasi199 – 28789Lys-richAdd
BLAST
Compositional biasi443 – 49149Ser-richAdd
BLAST
Compositional biasi559 – 60143Pro-richAdd
BLAST
Compositional biasi559 – 5624Poly-Pro
Compositional biasi566 – 5694Poly-Pro
Compositional biasi703 – 807105Ser-richAdd
BLAST
Compositional biasi1234 – 1366133Pro-richAdd
BLAST
Compositional biasi1819 – 186749Pro-richAdd
BLAST
Compositional biasi2185 – 2320136Ser-richAdd
BLAST

Domaini

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.By similarity
The CXXC-type zinc finger binds bind to nonmethyl-CpG dinucleotides.By similarity

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation
Contains 3 A.T hook DNA-binding domains.Curated
Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
Contains 1 FYR C-terminal domain.PROSITE-ProRule annotation
Contains 1 FYR N-terminal domain.PROSITE-ProRule annotation
Contains 3 PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1144 – 119249CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1430 – 148152PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1478 – 153255PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1565 – 162965PHD-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000119228.
HOGENOMiHOG000112954.
HOVERGENiHBG051927.
InParanoidiP55200.
KOiK09186.
OMAiRIMSPMR.
OrthoDBiEOG7XH6NX.
TreeFamiTF319820.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR001487. Bromodomain.
IPR003889. FYrich_C.
IPR003888. FYrich_N.
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.
[Graphical view]
PfamiPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
PIRSFiPIRSF010354. Methyltransferase_trithorax. 1 hit.
SMARTiSM00384. AT_hook. 3 hits.
SM00297. BROMO. 1 hit.
SM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00249. PHD. 4 hits.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEiPS50014. BROMODOMAIN_2. 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.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P55200-1) [UniParc]FASTAAdd to basket

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

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        10         20         30         40         50
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG
60 70 80 90 100
PGAPPSPPAV AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG
110 120 130 140 150
PALLRVGPGF DAALQVSAAI GTNLRRFRAV FGESGGGGGS GEDEQFLGFG
160 170 180 190 200
SDEEVRVRSP TRSPSVKASP RKPRGRPRSG SDRNPAILSD PSVFSPLNKS
210 220 230 240 250
ETKSADKIKK KDSKSIEKKR GRPPTFPGVK IKITHGKDIA ELTQGSKEDS
260 270 280 290 300
LKKVKRTPSA MFQQATKIKK LRAGKLSPLK SKFKTGKLQI GRKGVQIVRR
310 320 330 340 350
RGRPPSTERI KTPSGLLINS ELEKPQKVRK DKEGTPPLTK EDKTVVRQSP
360 370 380 390 400
RRIKPVRIIP SCKRTDATIA KQLLQRAKKG AQKKIEKEAA QLQGRKVKTQ
410 420 430 440 450
VKNIRQFIMP VVSAISSRII KTPRRFIEDE DYDPPMKIAR LESTPNSRFS
460 470 480 490 500
ATSCGSSEKS SAASQHSSQM SSDSSRSSSP SIDTTSDSQA SEEIQALPEE
510 520 530 540 550
RSNTPEVHTP LPISQSPENE SNDRRSRRYS MSERSFGSRA TKKLPTLQSA
560 570 580 590 600
PQQQTSSSPP PPLLTPPPPL QPASGISDHT PWLMPPTIPL ASPFLPASAA
610 620 630 640 650
PMQGKRKSIL REPTFRWTSL KHSRSEPQYF SSAKYAKEGL IRKPIFDNFR
660 670 680 690 700
PPPLTPEDVG FASGFSASGT AASARLFSPL HSGTRFDIHK RSPILRAPRF
710 720 730 740 750
TPSEAHSRIF ESVTLPSNRT SSGASSSGVS NRKRKRKVFS PIRSEPRSPS
760 770 780 790 800
HSMRTRSGRL STSELSPLTP PSSVSSSLSI PVSPLAASAL NPTFTFPSHS
810 820 830 840 850
LTQSGESTEK NQRARKQTSA LAEPFSSNSP ALFPWFTPGS QTEKGRKKDT
860 870 880 890 900
APEELSKDRD ADKSVEKDKS RERDREREKE NKRESRKEKR KKGSDIQSSS
910 920 930 940 950
ALYPVGRVSK EKVAGEDVGT SSSAKKATGR KKSSSLDSGA DVAPVTLGDT
960 970 980 990 1000
TAVKAKILIK KGRGNLEKNN LDLGPAAPSL EKERTPCLSA PSSSTVKHST
1010 1020 1030 1040 1050
SSIGSMLAQA DKLPMTDKRV ASLLKKAKAQ LCKIEKSKSL KQTDQPKAQG
1060 1070 1080 1090 1100
QESDSSETSV RGPRIKHVCR RAAVALGRKR AVFPDDMPTL SALPWEEREK
1110 1120 1130 1140 1150
ILSSMGNDDK SSVAGSEDAE PLAPPIKPIK PVTRNKAPQE PPVKKGRRSR
1160 1170 1180 1190 1200
RCGQCPGCQV PEDCGICTNC LDKPKFGGRN IKKQCCKMRK CQNLQWMPSK
1210 1220 1230 1240 1250
ASLQKQTKAV KKKEKKSKTT EKKESKESTA VKSPLEPAQK AAPPPREEPA
1260 1270 1280 1290 1300
PKKSSSEPPP RKPVEEKSEE GGAPAPAPAP EPKQVSAPAS RKSSKQVSQP
1310 1320 1330 1340 1350
AAVVPPQPPS TAPQKKEAPK AVPSEPKKKQ PPPPEPGPEQ SKQKKVAPRP
1360 1370 1380 1390 1400
SIPVKQKPKD KEKPPPVSKQ ENAGTLNILN PLSNGISSKQ KIPADGVHRI
1410 1420 1430 1440 1450
RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG HVEFVYCQVC
1460 1470 1480 1490 1500
CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC
1510 1520 1530 1540 1550
RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH
1560 1570 1580 1590 1600
DFSLCHDCAK LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCES
1610 1620 1630 1640 1650
LSGTEDEMYE ILSNLPESVA YTCVNCTERH PAEWRLALEK ELQASLKQVL
1660 1670 1680 1690 1700
TALLNSRTTS HLLRYRQAAK PPDLNPETEE SIPSRSSPEG PDPPVLTEVS
1710 1720 1730 1740 1750
KQDEQQPLDL EGVKKRMDQG SYVSVLEFSD DIVKIIQAAI NSDGGQPEIK
1760 1770 1780 1790 1800
KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSNNSGM LPNAVLPPSL
1810 1820 1830 1840 1850
DHNYAQWQER EESSHTEQPP LMKKIIPAPK PKGPGEPDSP TPLHPPTPPI
1860 1870 1880 1890 1900
LSTDRSREDS PELNPPPGID DNRQCALCLM YGDDSANDAG RLLYIGQNEW
1910 1920 1930 1940 1950
THVNCALWSA EVFEDDDGSL KNVHMAVIRG KQLRCEFCQK PGATVGCCLT
1960 1970 1980 1990 2000
SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR DLIKGEVVPE NGFEVFRRVF
2010 2020 2030 2040 2050
VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS DCEDKLFPIG
2060 2070 2080 2090 2100
YQCSRVYWST TDARKRCVYT CKIMECRPPV VEPDINSTVE HDDNRTIAHS
2110 2120 2130 2140 2150
PSSFIDASCK DSQSTAAILS PPSPDRPHSQ TSGSCYYHVI SKVPRIRTPS
2160 2170 2180 2190 2200
YSPTQRSPGC RPLPSAGSPT PTTHEIVTVG DPLLSSGLRS IGSRRHSTSS
2210 2220 2230 2240 2250
LSPLRSKLRI MSPVRTGSAY SRSSVSSVPS LGTATDPEAS AKASDRGGLL
2260 2270 2280 2290 2300
SSSANLGHSA PPSSSSQRTV GGSKTSHLDG SSPSEVKRCS ASDLVPKGSL
2310 2320 2330 2340 2350
VKGEKNRTSS SKSTDGSAHS TAYPGIPKLT PQVHNATPGE LNISKIGSFA
2360 2370 2380 2390 2400
EPSTVPFSSK DTVSYPQLHL RGQRSDRDQH MDPSQSVKPS PNEDGEIKTL
2410 2420 2430 2440 2450
KLPGMGHRPS ILHEHIGSSS RDRRQKGKKS SKETCKEKHS SKSYLEPGQV
2460 2470 2480 2490 2500
TTGEEGNLKP EFADEVLTPG FLGQRPCNNV SSEKIGDKVL PLSGVPKGQS
2510 2520 2530 2540 2550
TQVEGSSKEL QAPRKCSVKV TPLKMEGENQ SKNTQKESGP GSPAHIESVC
2560 2570 2580 2590 2600
PAEPVSASRS PGAGPGVQPS PNNTLSQDPQ SNNYQNLPEQ DRNLMIPDGP
2610 2620 2630 2640 2650
KPQEDGSFKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED IPFYSNSTGK
2660 2670 2680 2690 2700
KRGKRSAEGQ VDGADDLSTS DEDDLYYYNF TRTVISSGGE ERLASHNLFR
2710 2720 2730 2740 2750
EEEQCDLPKI SQLDGVDDGT ESDTSVTATS RKSSQIPKRN GKENGTENLK
2760 2770 2780 2790 2800
IDRPEDAGEK EHVIKSAVGH KNEPKLDNCH SVSRVKAQGQ DSLEAQLSSL
2810 2820 2830 2840 2850
ESSRRVHTST PSDKNLLDTY NAELLKSDSD NNNSDDCGNI LPSDIMDFVL
2860 2870 2880 2890 2900
KNTPSMQALG ESPESSSSEL LTLGEGLGLD SNREKDIGLF EVFSQQLPAT
2910 2920 2930 2940 2950
EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ NPSRLAVISD
2960 2970 2980 2990 3000
SGEKRVTITE KSVASSEGDP ALLSPGVDPA PEGHMTPDHF IQGHMDADHI
3010 3020 3030 3040 3050
SSPPCGSVEQ GHGNSQDLTR NSGTPGLQVP VSPTVPVQNQ KYVPSSTDSP
3060 3070 3080 3090 3100
GPSQISNAAV QTTPPHLKPA TEKLIVVNQN MQPLYVLQTL PNGVTQKIQL
3110 3120 3130 3140 3150
TSPVSSTPSV METNTSVLGP MGSGLTLTTG LNPSLPPSPS LFPPASKGLL
3160 3170 3180 3190 3200
SVPHHQHLHS FPAAAQSSFP PNISSPPSGL LIGVQPPPDP QLLGSEANQR
3210 3220 3230 3240 3250
TDLTTTVATP SSGLKKRPIS RLHTRKNKKL APSSAPSNIA PSDVVSNMTL
3260 3270 3280 3290 3300
INFTPSQLSN HPSLLDLGSL NPSSHRTVPN IIKRSKSGIM YFEQAPLLPP
3310 3320 3330 3340 3350
QSVGGTAATA AGSSTISQDT SHLTSGPVSA LASGSSVLNV VSMQTTAAPT
3360 3370 3380 3390 3400
SSTSVPGHVT LANQRLLGTP DIGSISHLLI KASHQSLGIQ DQPVALPPSS
3410 3420 3430 3440 3450
GMFPQLGTSQ TPSAAAMTAA SSICVLPSSQ TAGMTAASPP GEAEEHYKLQ
3460 3470 3480 3490 3500
RGNQLLAGKT GTLTSQRDRD PDSAPGTQPS NFTQTAEAPN GVRLEQNKTL
3510 3520 3530 3540 3550
PSAKPASSAS PGSSPSSGQQ SGSSSVPGPT KPKPKAKRIQ LPLDKGSGKK
3560 3570 3580 3590 3600
HKVSHLRTSS EAHIPHRDTD PAPQPSVTRT PRANREQQDA AGVEQPSQKE
3610 3620 3630 3640 3650
CGQPAGPVAA LPEVQATQNP ANEQENAEPK AMEEEESGFS SPLMLWLQQE
3660 3670 3680 3690 3700
QKRKESITER KPKKGLVFEI SSDDGFQICA ESIEDAWKSL TDKVQEARSN
3710 3720 3730 3740 3750
ARLKQLSFAG VNGLRMLGIL HDAVVFLIEQ LAGAKHCRNY KFRFHKPEEA
3760 3770 3780 3790 3800
NEPPLNPHGS ARAEVHLRQS AFDMFNFLAS KHRQPPEYNP NDEEEEEVQL
3810 3820 3830 3840 3850
KSARRATSMD LPMPMRFRHL KKTSKEAVGV YRSPIHGRGL FCKRNIDAGE
3860 3870 3880 3890 3900
MVIEYAGNVI RSIQTDKREK YYDSKGIGCY MFRIDDSEVV DATMHGNAAR
3910 3920 3930 3940 3950
FINHSCEPNC YSRVINIDGQ KHIVIFAMRK IYRGEELTYD YKFPIEDASN
3960
KLPCNCGAKK CRKFLN
Length:3,966
Mass (Da):429,649
Last modified:July 27, 2011 - v3
Checksum:iEA9CB2A467AB3545
GO
Isoform 2 (identifier: P55200-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1603-1605: Missing.

Show »
Length:3,963
Mass (Da):429,362
Checksum:i5E5106EB6EF1B932
GO

Sequence cautioni

The sequence BAE24386.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti372 – 3721Q → E in BAE28820 (PubMed:16141072).Curated
Sequence conflicti554 – 5541Q → K in AAA62593 (PubMed:8327517).Curated
Sequence conflicti564 – 5641L → F in AAA62593 (PubMed:8327517).Curated
Sequence conflicti797 – 7971P → S in BAE28820 (PubMed:16141072).Curated
Sequence conflicti806 – 8061E → D in AAA62593 (PubMed:8327517).Curated
Sequence conflicti806 – 8061E → D in BAE28820 (PubMed:16141072).Curated
Sequence conflicti821 – 8211L → P in AAA62593 (PubMed:8327517).Curated
Sequence conflicti821 – 8211L → P in BAE28820 (PubMed:16141072).Curated
Sequence conflicti1069 – 10691C → Y in AAA62593 (PubMed:8327517).Curated
Sequence conflicti1230 – 12301A → S in AAA62593 (PubMed:8327517).Curated
Sequence conflicti1349 – 13491R → L in AAA62593 (PubMed:8327517).Curated
Sequence conflicti1437 – 14371A → S in AAA62593 (PubMed:8327517).Curated
Sequence conflicti1440 – 14401G → E in AAA62593 (PubMed:8327517).Curated
Sequence conflicti1632 – 16321A → P in AAA62593 (PubMed:8327517).Curated
Sequence conflicti2292 – 22921S → L in AAA62593 (PubMed:8327517).Curated
Sequence conflicti3481 – 34811N → I in AAA62593 (PubMed:8327517).Curated
Sequence conflicti3493 – 34931R → S in AAA62593 (PubMed:8327517).Curated
Sequence conflicti3548 – 35481G → V in AAA62593 (PubMed:8327517).Curated
Sequence conflicti3769 – 37691Q → K in AAA62593 (PubMed:8327517).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1597 – 15971K → T.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1603 – 16053Missing in isoform 2. 1 PublicationVSP_006667

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC061963 Genomic DNA. No translation available.
AC142113 Genomic DNA. No translation available.
L17069 mRNA. Translation: AAA62593.1.
AK140439 mRNA. Translation: BAE24386.1. Different initiation.
AK149341 mRNA. Translation: BAE28820.1.
CCDSiCCDS40603.1. [P55200-2]
RefSeqiNP_001074518.1. NM_001081049.1. [P55200-2]
UniGeneiMm.2389.

Genome annotation databases

EnsembliENSMUST00000002095; ENSMUSP00000002095; ENSMUSG00000002028. [P55200-2]
ENSMUST00000114689; ENSMUSP00000110337; ENSMUSG00000002028. [P55200-1]
GeneIDi214162.
KEGGimmu:214162.
UCSCiuc009pep.1. mouse. [P55200-2]
uc009peq.1. mouse. [P55200-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC061963 Genomic DNA. No translation available.
AC142113 Genomic DNA. No translation available.
L17069 mRNA. Translation: AAA62593.1.
AK140439 mRNA. Translation: BAE24386.1. Different initiation.
AK149341 mRNA. Translation: BAE28820.1.
CCDSiCCDS40603.1. [P55200-2]
RefSeqiNP_001074518.1. NM_001081049.1. [P55200-2]
UniGeneiMm.2389.

3D structure databases

ProteinModelPortaliP55200.
SMRiP55200. Positions 6-39, 101-133, 1147-1197, 1563-1781, 2836-2865, 3787-3966.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58597N.
IntActiP55200. 1 interaction.
MINTiMINT-4084570.

PTM databases

PhosphoSiteiP55200.

Proteomic databases

MaxQBiP55200.
PaxDbiP55200.
PRIDEiP55200.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002095; ENSMUSP00000002095; ENSMUSG00000002028. [P55200-2]
ENSMUST00000114689; ENSMUSP00000110337; ENSMUSG00000002028. [P55200-1]
GeneIDi214162.
KEGGimmu:214162.
UCSCiuc009pep.1. mouse. [P55200-2]
uc009peq.1. mouse. [P55200-1]

Organism-specific databases

CTDi4297.
MGIiMGI:96995. Kmt2a.

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000119228.
HOGENOMiHOG000112954.
HOVERGENiHBG051927.
InParanoidiP55200.
KOiK09186.
OMAiRIMSPMR.
OrthoDBiEOG7XH6NX.
TreeFamiTF319820.

Miscellaneous databases

NextBioi374214.
PROiP55200.
SOURCEiSearch...

Gene expression databases

BgeeiP55200.
CleanExiMM_MLL1.
ExpressionAtlasiP55200. baseline and differential.
GenevestigatoriP55200.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR001487. Bromodomain.
IPR003889. FYrich_C.
IPR003888. FYrich_N.
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.
[Graphical view]
PfamiPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
PIRSFiPIRSF010354. Methyltransferase_trithorax. 1 hit.
SMARTiSM00384. AT_hook. 3 hits.
SM00297. BROMO. 1 hit.
SM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00249. PHD. 4 hits.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEiPS50014. BROMODOMAIN_2. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "Analysis of the murine All-1 gene reveals conserved domains with human ALL-1 and identifies a motif shared with DNA methyltransferases."
    Ma Q., Alder H., Nelson K.K., Chatterjee D., Gu Y., Nakamura T., Canaani E., Croce C.M., Siracusa L.D., Buchberg A.M.
    Proc. Natl. Acad. Sci. U.S.A. 90:6350-6354(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-3966 (ISOFORMS 1 AND 2).
    Strain: C57BL/6 X CBA and C57BL/6J.
    Tissue: Lung and Spleen.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 372-1517 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Medulla oblongata and Retina.
  4. "The histone methyltransferase MLL1 permits the oscillation of circadian gene expression."
    Katada S., Sassone-Corsi P.
    Nat. Struct. Mol. Biol. 17:1414-1421(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLOCK AND ARNTL.
  5. "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains."
    Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.
    Cell 144:513-525(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN MLL COMPLEX, INTERACTION WITH ASH2L; DPY30; KMT2D; RRBP5 AND WDR5.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237; LYS-371; LYS-2954 AND LYS-3459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiKMT2A_MOUSE
AccessioniPrimary (citable) accession number: P55200
Secondary accession number(s): E9QNE7, Q3UEU1, Q3USE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: March 4, 2015
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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