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P55200 (KMT2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase 2A

Short name=Lysine N-methyltransferase 2A
EC=2.1.1.43
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:

  1. MLL cleavage product N320
    Alternative name(s):
    N-terminal cleavage product of 320 kDa
    Short name=p320
  2. MLL cleavage product C180
    Alternative name(s):
    C-terminal cleavage product of 180 kDa
    Short name=p180
Gene names
Name:Kmt2a
Synonyms:All1, Hrx, Mll, Mll1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3966 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

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. Ref.4

Subcellular location

Nucleus By similarity.

MLL cleavage product N320: Nucleus By similarity.

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

Domain

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.

Post-translational modification

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.

Sequence similarities

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

Contains 3 A.T hook DNA-binding domains.

Contains 1 bromo domain.

Contains 1 CXXC-type zinc finger.

Contains 1 FYR C-terminal domain.

Contains 1 FYR N-terminal domain.

Contains 3 PHD-type zinc fingers.

Contains 1 post-SET domain.

Contains 1 SET domain.

Sequence caution

The sequence BAE24386.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainBromodomain
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from mutant phenotype PubMed 16618927. Source: MGI

anterior/posterior pattern specification

Inferred from mutant phenotype PubMed 16618927. Source: MGI

embryonic hemopoiesis

Inferred from mutant phenotype PubMed 9639506. Source: MGI

histone H3-K4 methylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3-K4 trimethylation

Inferred from electronic annotation. Source: Ensembl

histone H4-K16 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 15640349. Source: MGI

positive regulation of cellular response to drug

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 15640349. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transporter activity

Inferred from electronic annotation. Source: Ensembl

protein complex assembly

Inferred from electronic annotation. Source: Ensembl

regulation of histone H3-K4 methylation

Inferred from mutant phenotype PubMed 16618927. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

histone methyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 11555636PubMed 16618927. Source: MGI

   Molecular_functionchromatin binding

Inferred from direct assay PubMed 15640349. Source: MGI

histone methyltransferase activity (H3-K4 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

lysine-acetylated histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16618927. Source: MGI

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

unmethylated CpG binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55200-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P55200-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 39663966Histone-lysine N-methyltransferase 2A
PRO_0000124877
Chain1 – 27142714MLL cleavage product N320 By similarity
PRO_0000390951
Chain2715 – 39661252MLL cleavage product C180 By similarity
PRO_0000390952

Regions

Domain1705 – 175046Bromo; divergent
Domain2020 – 207657FYR N-terminal
Domain3663 – 374482FYR C-terminal
Domain3826 – 3942117SET
Domain3950 – 396617Post-SET
DNA binding167 – 17812A.T hook 1
DNA binding215 – 22511A.T hook 2
DNA binding299 – 3079A.T hook 3
Zinc finger1144 – 119249CXXC-type
Zinc finger1430 – 148152PHD-type 1
Zinc finger1478 – 153255PHD-type 2
Zinc finger1565 – 162965PHD-type 3
Region3903 – 39042S-adenosyl-L-methionine binding By similarity
Compositional bias14 – 150137Gly-rich
Compositional bias17 – 10084Ala/Gly/Ser-rich
Compositional bias80 – 9920Ser-rich
Compositional bias135 – 1417Poly-Gly
Compositional bias199 – 28789Lys-rich
Compositional bias443 – 49149Ser-rich
Compositional bias559 – 60143Pro-rich
Compositional bias559 – 5624Poly-Pro
Compositional bias566 – 5694Poly-Pro
Compositional bias703 – 807105Ser-rich
Compositional bias1234 – 1366133Pro-rich
Compositional bias1819 – 186749Pro-rich
Compositional bias2185 – 2320136Ser-rich

Sites

Metal binding39061Zinc By similarity
Metal binding39541Zinc By similarity
Metal binding39561Zinc By similarity
Metal binding39611Zinc By similarity
Binding site38361S-adenosyl-L-methionine By similarity
Binding site38381S-adenosyl-L-methionine By similarity
Binding site38801S-adenosyl-L-methionine By similarity
Binding site39551S-adenosyl-L-methionine By similarity
Site2662 – 26632Cleavage; by TASP1, site 1 By similarity
Site2714 – 27152Cleavage; by TASP1, site 2 By similarity
Site37621Important for WDR5-recognition and binding By similarity

Amino acid modifications

Modified residue1511Phosphoserine By similarity
Modified residue1951Phosphoserine By similarity
Modified residue2371N6-acetyllysine Ref.5
Modified residue3711N6-acetyllysine Ref.5
Modified residue5161Phosphoserine By similarity
Modified residue6341N6-acetyllysine By similarity
Modified residue6781Phosphoserine By similarity
Modified residue8371Phosphothreonine By similarity
Modified residue9231Phosphoserine By similarity
Modified residue10531Phosphoserine By similarity
Modified residue11271N6-acetyllysine By similarity
Modified residue12321N6-acetyllysine By similarity
Modified residue18471Phosphothreonine By similarity
Modified residue18601Phosphoserine By similarity
Modified residue21001Phosphoserine By similarity
Modified residue21481Phosphothreonine By similarity
Modified residue21521Phosphoserine By similarity
Modified residue22021Phosphoserine By similarity
Modified residue29511Phosphoserine By similarity
Modified residue29541N6-acetyllysine Ref.5
Modified residue30321Phosphoserine By similarity
Modified residue33691Phosphothreonine By similarity
Modified residue34591N6-acetyllysine Ref.5
Modified residue35101Phosphoserine By similarity
Cross-link214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link218Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence1603 – 16053Missing in isoform 2.
VSP_006667
Natural variant15971K → T.

Experimental info

Sequence conflict3721Q → E in BAE28820. Ref.3
Sequence conflict5541Q → K in AAA62593. Ref.2
Sequence conflict5641L → F in AAA62593. Ref.2
Sequence conflict7971P → S in BAE28820. Ref.3
Sequence conflict8061E → D in AAA62593. Ref.2
Sequence conflict8061E → D in BAE28820. Ref.3
Sequence conflict8211L → P in AAA62593. Ref.2
Sequence conflict8211L → P in BAE28820. Ref.3
Sequence conflict10691C → Y in AAA62593. Ref.2
Sequence conflict12301A → S in AAA62593. Ref.2
Sequence conflict13491R → L in AAA62593. Ref.2
Sequence conflict14371A → S in AAA62593. Ref.2
Sequence conflict14401G → E in AAA62593. Ref.2
Sequence conflict16321A → P in AAA62593. Ref.2
Sequence conflict22921S → L in AAA62593. Ref.2
Sequence conflict34811N → I in AAA62593. Ref.2
Sequence conflict34931R → S in AAA62593. Ref.2
Sequence conflict35481G → V in AAA62593. Ref.2
Sequence conflict37691Q → K in AAA62593. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: EA9CB2A467AB3545

FASTA3,966429,649
        10         20         30         40         50         60 
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG PGAPPSPPAV 

        70         80         90        100        110        120 
AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG PALLRVGPGF DAALQVSAAI 

       130        140        150        160        170        180 
GTNLRRFRAV FGESGGGGGS GEDEQFLGFG SDEEVRVRSP TRSPSVKASP RKPRGRPRSG 

       190        200        210        220        230        240 
SDRNPAILSD PSVFSPLNKS ETKSADKIKK KDSKSIEKKR GRPPTFPGVK IKITHGKDIA 

       250        260        270        280        290        300 
ELTQGSKEDS LKKVKRTPSA MFQQATKIKK LRAGKLSPLK SKFKTGKLQI GRKGVQIVRR 

       310        320        330        340        350        360 
RGRPPSTERI KTPSGLLINS ELEKPQKVRK DKEGTPPLTK EDKTVVRQSP RRIKPVRIIP 

       370        380        390        400        410        420 
SCKRTDATIA KQLLQRAKKG AQKKIEKEAA QLQGRKVKTQ VKNIRQFIMP VVSAISSRII 

       430        440        450        460        470        480 
KTPRRFIEDE DYDPPMKIAR LESTPNSRFS ATSCGSSEKS SAASQHSSQM SSDSSRSSSP 

       490        500        510        520        530        540 
SIDTTSDSQA SEEIQALPEE RSNTPEVHTP LPISQSPENE SNDRRSRRYS MSERSFGSRA 

       550        560        570        580        590        600 
TKKLPTLQSA PQQQTSSSPP PPLLTPPPPL QPASGISDHT PWLMPPTIPL ASPFLPASAA 

       610        620        630        640        650        660 
PMQGKRKSIL REPTFRWTSL KHSRSEPQYF SSAKYAKEGL IRKPIFDNFR PPPLTPEDVG 

       670        680        690        700        710        720 
FASGFSASGT AASARLFSPL HSGTRFDIHK RSPILRAPRF TPSEAHSRIF ESVTLPSNRT 

       730        740        750        760        770        780 
SSGASSSGVS NRKRKRKVFS PIRSEPRSPS HSMRTRSGRL STSELSPLTP PSSVSSSLSI 

       790        800        810        820        830        840 
PVSPLAASAL NPTFTFPSHS LTQSGESTEK NQRARKQTSA LAEPFSSNSP ALFPWFTPGS 

       850        860        870        880        890        900 
QTEKGRKKDT APEELSKDRD ADKSVEKDKS RERDREREKE NKRESRKEKR KKGSDIQSSS 

       910        920        930        940        950        960 
ALYPVGRVSK EKVAGEDVGT SSSAKKATGR KKSSSLDSGA DVAPVTLGDT TAVKAKILIK 

       970        980        990       1000       1010       1020 
KGRGNLEKNN LDLGPAAPSL EKERTPCLSA PSSSTVKHST SSIGSMLAQA DKLPMTDKRV 

      1030       1040       1050       1060       1070       1080 
ASLLKKAKAQ LCKIEKSKSL KQTDQPKAQG QESDSSETSV RGPRIKHVCR RAAVALGRKR 

      1090       1100       1110       1120       1130       1140 
AVFPDDMPTL SALPWEEREK ILSSMGNDDK SSVAGSEDAE PLAPPIKPIK PVTRNKAPQE 

      1150       1160       1170       1180       1190       1200 
PPVKKGRRSR RCGQCPGCQV PEDCGICTNC LDKPKFGGRN IKKQCCKMRK CQNLQWMPSK 

      1210       1220       1230       1240       1250       1260 
ASLQKQTKAV KKKEKKSKTT EKKESKESTA VKSPLEPAQK AAPPPREEPA PKKSSSEPPP 

      1270       1280       1290       1300       1310       1320 
RKPVEEKSEE GGAPAPAPAP EPKQVSAPAS RKSSKQVSQP AAVVPPQPPS TAPQKKEAPK 

      1330       1340       1350       1360       1370       1380 
AVPSEPKKKQ PPPPEPGPEQ SKQKKVAPRP SIPVKQKPKD KEKPPPVSKQ ENAGTLNILN 

      1390       1400       1410       1420       1430       1440 
PLSNGISSKQ KIPADGVHRI RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG 

      1450       1460       1470       1480       1490       1500 
HVEFVYCQVC CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC 

      1510       1520       1530       1540       1550       1560 
RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH DFSLCHDCAK 

      1570       1580       1590       1600       1610       1620 
LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCES LSGTEDEMYE ILSNLPESVA 

      1630       1640       1650       1660       1670       1680 
YTCVNCTERH PAEWRLALEK ELQASLKQVL TALLNSRTTS HLLRYRQAAK PPDLNPETEE 

      1690       1700       1710       1720       1730       1740 
SIPSRSSPEG PDPPVLTEVS KQDEQQPLDL EGVKKRMDQG SYVSVLEFSD DIVKIIQAAI 

      1750       1760       1770       1780       1790       1800 
NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSNNSGM LPNAVLPPSL 

      1810       1820       1830       1840       1850       1860 
DHNYAQWQER EESSHTEQPP LMKKIIPAPK PKGPGEPDSP TPLHPPTPPI LSTDRSREDS 

      1870       1880       1890       1900       1910       1920 
PELNPPPGID DNRQCALCLM YGDDSANDAG RLLYIGQNEW THVNCALWSA EVFEDDDGSL 

      1930       1940       1950       1960       1970       1980 
KNVHMAVIRG KQLRCEFCQK PGATVGCCLT SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR 

      1990       2000       2010       2020       2030       2040 
DLIKGEVVPE NGFEVFRRVF VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS 

      2050       2060       2070       2080       2090       2100 
DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIMECRPPV VEPDINSTVE HDDNRTIAHS 

      2110       2120       2130       2140       2150       2160 
PSSFIDASCK DSQSTAAILS PPSPDRPHSQ TSGSCYYHVI SKVPRIRTPS YSPTQRSPGC 

      2170       2180       2190       2200       2210       2220 
RPLPSAGSPT PTTHEIVTVG DPLLSSGLRS IGSRRHSTSS LSPLRSKLRI MSPVRTGSAY 

      2230       2240       2250       2260       2270       2280 
SRSSVSSVPS LGTATDPEAS AKASDRGGLL SSSANLGHSA PPSSSSQRTV GGSKTSHLDG 

      2290       2300       2310       2320       2330       2340 
SSPSEVKRCS ASDLVPKGSL VKGEKNRTSS SKSTDGSAHS TAYPGIPKLT PQVHNATPGE 

      2350       2360       2370       2380       2390       2400 
LNISKIGSFA EPSTVPFSSK DTVSYPQLHL RGQRSDRDQH MDPSQSVKPS PNEDGEIKTL 

      2410       2420       2430       2440       2450       2460 
KLPGMGHRPS ILHEHIGSSS RDRRQKGKKS SKETCKEKHS SKSYLEPGQV TTGEEGNLKP 

      2470       2480       2490       2500       2510       2520 
EFADEVLTPG FLGQRPCNNV SSEKIGDKVL PLSGVPKGQS TQVEGSSKEL QAPRKCSVKV 

      2530       2540       2550       2560       2570       2580 
TPLKMEGENQ SKNTQKESGP GSPAHIESVC PAEPVSASRS PGAGPGVQPS PNNTLSQDPQ 

      2590       2600       2610       2620       2630       2640 
SNNYQNLPEQ DRNLMIPDGP KPQEDGSFKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED 

      2650       2660       2670       2680       2690       2700 
IPFYSNSTGK KRGKRSAEGQ VDGADDLSTS DEDDLYYYNF TRTVISSGGE ERLASHNLFR 

      2710       2720       2730       2740       2750       2760 
EEEQCDLPKI SQLDGVDDGT ESDTSVTATS RKSSQIPKRN GKENGTENLK IDRPEDAGEK 

      2770       2780       2790       2800       2810       2820 
EHVIKSAVGH KNEPKLDNCH SVSRVKAQGQ DSLEAQLSSL ESSRRVHTST PSDKNLLDTY 

      2830       2840       2850       2860       2870       2880 
NAELLKSDSD NNNSDDCGNI LPSDIMDFVL KNTPSMQALG ESPESSSSEL LTLGEGLGLD 

      2890       2900       2910       2920       2930       2940 
SNREKDIGLF EVFSQQLPAT EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ 

      2950       2960       2970       2980       2990       3000 
NPSRLAVISD SGEKRVTITE KSVASSEGDP ALLSPGVDPA PEGHMTPDHF IQGHMDADHI 

      3010       3020       3030       3040       3050       3060 
SSPPCGSVEQ GHGNSQDLTR NSGTPGLQVP VSPTVPVQNQ KYVPSSTDSP GPSQISNAAV 

      3070       3080       3090       3100       3110       3120 
QTTPPHLKPA TEKLIVVNQN MQPLYVLQTL PNGVTQKIQL TSPVSSTPSV METNTSVLGP 

      3130       3140       3150       3160       3170       3180 
MGSGLTLTTG LNPSLPPSPS LFPPASKGLL SVPHHQHLHS FPAAAQSSFP PNISSPPSGL 

      3190       3200       3210       3220       3230       3240 
LIGVQPPPDP QLLGSEANQR TDLTTTVATP SSGLKKRPIS RLHTRKNKKL APSSAPSNIA 

      3250       3260       3270       3280       3290       3300 
PSDVVSNMTL INFTPSQLSN HPSLLDLGSL NPSSHRTVPN IIKRSKSGIM YFEQAPLLPP 

      3310       3320       3330       3340       3350       3360 
QSVGGTAATA AGSSTISQDT SHLTSGPVSA LASGSSVLNV VSMQTTAAPT SSTSVPGHVT 

      3370       3380       3390       3400       3410       3420 
LANQRLLGTP DIGSISHLLI KASHQSLGIQ DQPVALPPSS GMFPQLGTSQ TPSAAAMTAA 

      3430       3440       3450       3460       3470       3480 
SSICVLPSSQ TAGMTAASPP GEAEEHYKLQ RGNQLLAGKT GTLTSQRDRD PDSAPGTQPS 

      3490       3500       3510       3520       3530       3540 
NFTQTAEAPN GVRLEQNKTL PSAKPASSAS PGSSPSSGQQ SGSSSVPGPT KPKPKAKRIQ 

      3550       3560       3570       3580       3590       3600 
LPLDKGSGKK HKVSHLRTSS EAHIPHRDTD PAPQPSVTRT PRANREQQDA AGVEQPSQKE 

      3610       3620       3630       3640       3650       3660 
CGQPAGPVAA LPEVQATQNP ANEQENAEPK AMEEEESGFS SPLMLWLQQE QKRKESITER 

      3670       3680       3690       3700       3710       3720 
KPKKGLVFEI SSDDGFQICA ESIEDAWKSL TDKVQEARSN ARLKQLSFAG VNGLRMLGIL 

      3730       3740       3750       3760       3770       3780 
HDAVVFLIEQ LAGAKHCRNY KFRFHKPEEA NEPPLNPHGS ARAEVHLRQS AFDMFNFLAS 

      3790       3800       3810       3820       3830       3840 
KHRQPPEYNP NDEEEEEVQL KSARRATSMD LPMPMRFRHL KKTSKEAVGV YRSPIHGRGL 

      3850       3860       3870       3880       3890       3900 
FCKRNIDAGE MVIEYAGNVI RSIQTDKREK YYDSKGIGCY MFRIDDSEVV DATMHGNAAR 

      3910       3920       3930       3940       3950       3960 
FINHSCEPNC YSRVINIDGQ KHIVIFAMRK IYRGEELTYD YKFPIEDASN KLPCNCGAKK 


CRKFLN 

« Hide

Isoform 2 [UniParc].

Checksum: 5E5106EB6EF1B932
Show »

FASTA3,963429,362

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"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.
[5]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS40603.1. [P55200-2]
RefSeqNP_001074518.1. NM_001081049.1. [P55200-2]
UniGeneMm.2389.

3D structure databases

ProteinModelPortalP55200.
SMRP55200. Positions 6-39, 101-133, 1144-1200, 1563-1781, 2836-2865, 3787-3966.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-58597N.
IntActP55200. 1 interaction.
MINTMINT-4084570.

PTM databases

PhosphoSiteP55200.

Proteomic databases

PaxDbP55200.
PRIDEP55200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002095; ENSMUSP00000002095; ENSMUSG00000002028. [P55200-2]
ENSMUST00000114689; ENSMUSP00000110337; ENSMUSG00000002028. [P55200-1]
GeneID214162.
KEGGmmu:214162.
UCSCuc009pep.1. mouse. [P55200-2]
uc009peq.1. mouse. [P55200-1]

Organism-specific databases

CTD4297.
MGIMGI:96995. Kmt2a.

Phylogenomic databases

eggNOGCOG2940.
GeneTreeENSGT00740000115089.
HOGENOMHOG000112954.
HOVERGENHBG051927.
InParanoidP55200.
KOK09186.
OMARIMSPMR.
OrthoDBEOG7XH6NX.
TreeFamTF319820.

Gene expression databases

ArrayExpressP55200.
BgeeP55200.
CleanExMM_MLL1.
GenevestigatorP55200.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
InterProIPR017956. 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]
PfamPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
PIRSFPIRSF010354. Methyltransferase_trithorax. 1 hit.
SMARTSM00384. 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]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEPS50014. 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]
ProtoNetSearch...

Other

NextBio374214.
PROP55200.
SOURCESearch...

Entry information

Entry nameKMT2A_MOUSE
AccessionPrimary (citable) accession number: P55200
Secondary accession number(s): E9QNE7, Q3UEU1, Q3USE7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot