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P55200

- KMT2A_MOUSE

UniProt

P55200 - KMT2A_MOUSE

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Protein

Histone-lysine N-methyltransferase 2A

Gene
Kmt2a, All1, Hrx, Mll, Mll1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

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 1 By similarity
Sitei2714 – 27152Cleavage; by TASP1, site 2 By similarity
Sitei3762 – 37621Important for WDR5-recognition and binding By similarity
Binding sitei3836 – 38361S-adenosyl-L-methionine By similarity
Binding sitei3838 – 38381S-adenosyl-L-methionine By similarity
Binding sitei3880 – 38801S-adenosyl-L-methionine By similarity
Metal bindingi3906 – 39061Zinc By similarity
Metal bindingi3954 – 39541Zinc By similarity
Binding sitei3955 – 39551S-adenosyl-L-methionine By similarity
Metal bindingi3956 – 39561Zinc By similarity
Metal bindingi3961 – 39611Zinc By 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-typeAdd
BLAST
Zinc fingeri1430 – 148152PHD-type 1Add
BLAST
Zinc fingeri1478 – 153255PHD-type 2Add
BLAST
Zinc fingeri1565 – 162965PHD-type 3Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

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. histone methyltransferase complex Source: UniProtKB
  2. MLL1 complex Source: UniProtKB
  3. 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 N320 By similarityPRO_0000390951Add
BLAST
Chaini2715 – 39661252MLL cleavage product C180 By similarityPRO_0000390952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei151 – 1511Phosphoserine By similarity
Modified residuei195 – 1951Phosphoserine By 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 – 5161Phosphoserine By similarity
Modified residuei634 – 6341N6-acetyllysine By similarity
Modified residuei678 – 6781Phosphoserine By similarity
Modified residuei837 – 8371Phosphothreonine By similarity
Modified residuei923 – 9231Phosphoserine By similarity
Modified residuei1053 – 10531Phosphoserine By similarity
Modified residuei1127 – 11271N6-acetyllysine By similarity
Modified residuei1232 – 12321N6-acetyllysine By similarity
Modified residuei1847 – 18471Phosphothreonine By similarity
Modified residuei1860 – 18601Phosphoserine By similarity
Modified residuei2100 – 21001Phosphoserine By similarity
Modified residuei2148 – 21481Phosphothreonine By similarity
Modified residuei2152 – 21521Phosphoserine By similarity
Modified residuei2202 – 22021Phosphoserine By similarity
Modified residuei2951 – 29511Phosphoserine By similarity
Modified residuei2954 – 29541N6-acetyllysine1 Publication
Modified residuei3032 – 30321Phosphoserine By similarity
Modified residuei3369 – 33691Phosphothreonine By similarity
Modified residuei3459 – 34591N6-acetyllysine1 Publication
Modified residuei3510 – 35101Phosphoserine By 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

PaxDbiP55200.
PRIDEiP55200.

PTM databases

PhosphoSiteiP55200.

Expressioni

Gene expression databases

ArrayExpressiP55200.
BgeeiP55200.
CleanExiMM_MLL1.
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 TEX10.1 Publication

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP55200.
SMRiP55200. Positions 6-39, 101-133, 1144-1200, 1563-1781, 2836-2865, 3787-3966.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1705 – 175046Bromo; divergentAdd
BLAST
Domaini2020 – 207657FYR N-terminalAdd
BLAST
Domaini3663 – 374482FYR C-terminalAdd
BLAST
Domaini3826 – 3942117SETAdd
BLAST
Domaini3950 – 396617Post-SETAdd
BLAST

Region

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

Contains 1 bromo domain.
Contains 1 post-SET domain.
Contains 1 SET domain.

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00740000115089.
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. Align

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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MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG     50
PGAPPSPPAV AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG 100
PALLRVGPGF DAALQVSAAI GTNLRRFRAV FGESGGGGGS GEDEQFLGFG 150
SDEEVRVRSP TRSPSVKASP RKPRGRPRSG SDRNPAILSD PSVFSPLNKS 200
ETKSADKIKK KDSKSIEKKR GRPPTFPGVK IKITHGKDIA ELTQGSKEDS 250
LKKVKRTPSA MFQQATKIKK LRAGKLSPLK SKFKTGKLQI GRKGVQIVRR 300
RGRPPSTERI KTPSGLLINS ELEKPQKVRK DKEGTPPLTK EDKTVVRQSP 350
RRIKPVRIIP SCKRTDATIA KQLLQRAKKG AQKKIEKEAA QLQGRKVKTQ 400
VKNIRQFIMP VVSAISSRII KTPRRFIEDE DYDPPMKIAR LESTPNSRFS 450
ATSCGSSEKS SAASQHSSQM SSDSSRSSSP SIDTTSDSQA SEEIQALPEE 500
RSNTPEVHTP LPISQSPENE SNDRRSRRYS MSERSFGSRA TKKLPTLQSA 550
PQQQTSSSPP PPLLTPPPPL QPASGISDHT PWLMPPTIPL ASPFLPASAA 600
PMQGKRKSIL REPTFRWTSL KHSRSEPQYF SSAKYAKEGL IRKPIFDNFR 650
PPPLTPEDVG FASGFSASGT AASARLFSPL HSGTRFDIHK RSPILRAPRF 700
TPSEAHSRIF ESVTLPSNRT SSGASSSGVS NRKRKRKVFS PIRSEPRSPS 750
HSMRTRSGRL STSELSPLTP PSSVSSSLSI PVSPLAASAL NPTFTFPSHS 800
LTQSGESTEK NQRARKQTSA LAEPFSSNSP ALFPWFTPGS QTEKGRKKDT 850
APEELSKDRD ADKSVEKDKS RERDREREKE NKRESRKEKR KKGSDIQSSS 900
ALYPVGRVSK EKVAGEDVGT SSSAKKATGR KKSSSLDSGA DVAPVTLGDT 950
TAVKAKILIK KGRGNLEKNN LDLGPAAPSL EKERTPCLSA PSSSTVKHST 1000
SSIGSMLAQA DKLPMTDKRV ASLLKKAKAQ LCKIEKSKSL KQTDQPKAQG 1050
QESDSSETSV RGPRIKHVCR RAAVALGRKR AVFPDDMPTL SALPWEEREK 1100
ILSSMGNDDK SSVAGSEDAE PLAPPIKPIK PVTRNKAPQE PPVKKGRRSR 1150
RCGQCPGCQV PEDCGICTNC LDKPKFGGRN IKKQCCKMRK CQNLQWMPSK 1200
ASLQKQTKAV KKKEKKSKTT EKKESKESTA VKSPLEPAQK AAPPPREEPA 1250
PKKSSSEPPP RKPVEEKSEE GGAPAPAPAP EPKQVSAPAS RKSSKQVSQP 1300
AAVVPPQPPS TAPQKKEAPK AVPSEPKKKQ PPPPEPGPEQ SKQKKVAPRP 1350
SIPVKQKPKD KEKPPPVSKQ ENAGTLNILN PLSNGISSKQ KIPADGVHRI 1400
RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG HVEFVYCQVC 1450
CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC 1500
RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH 1550
DFSLCHDCAK LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCES 1600
LSGTEDEMYE ILSNLPESVA YTCVNCTERH PAEWRLALEK ELQASLKQVL 1650
TALLNSRTTS HLLRYRQAAK PPDLNPETEE SIPSRSSPEG PDPPVLTEVS 1700
KQDEQQPLDL EGVKKRMDQG SYVSVLEFSD DIVKIIQAAI NSDGGQPEIK 1750
KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSNNSGM LPNAVLPPSL 1800
DHNYAQWQER EESSHTEQPP LMKKIIPAPK PKGPGEPDSP TPLHPPTPPI 1850
LSTDRSREDS PELNPPPGID DNRQCALCLM YGDDSANDAG RLLYIGQNEW 1900
THVNCALWSA EVFEDDDGSL KNVHMAVIRG KQLRCEFCQK PGATVGCCLT 1950
SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR DLIKGEVVPE NGFEVFRRVF 2000
VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS DCEDKLFPIG 2050
YQCSRVYWST TDARKRCVYT CKIMECRPPV VEPDINSTVE HDDNRTIAHS 2100
PSSFIDASCK DSQSTAAILS PPSPDRPHSQ TSGSCYYHVI SKVPRIRTPS 2150
YSPTQRSPGC RPLPSAGSPT PTTHEIVTVG DPLLSSGLRS IGSRRHSTSS 2200
LSPLRSKLRI MSPVRTGSAY SRSSVSSVPS LGTATDPEAS AKASDRGGLL 2250
SSSANLGHSA PPSSSSQRTV GGSKTSHLDG SSPSEVKRCS ASDLVPKGSL 2300
VKGEKNRTSS SKSTDGSAHS TAYPGIPKLT PQVHNATPGE LNISKIGSFA 2350
EPSTVPFSSK DTVSYPQLHL RGQRSDRDQH MDPSQSVKPS PNEDGEIKTL 2400
KLPGMGHRPS ILHEHIGSSS RDRRQKGKKS SKETCKEKHS SKSYLEPGQV 2450
TTGEEGNLKP EFADEVLTPG FLGQRPCNNV SSEKIGDKVL PLSGVPKGQS 2500
TQVEGSSKEL QAPRKCSVKV TPLKMEGENQ SKNTQKESGP GSPAHIESVC 2550
PAEPVSASRS PGAGPGVQPS PNNTLSQDPQ SNNYQNLPEQ DRNLMIPDGP 2600
KPQEDGSFKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED IPFYSNSTGK 2650
KRGKRSAEGQ VDGADDLSTS DEDDLYYYNF TRTVISSGGE ERLASHNLFR 2700
EEEQCDLPKI SQLDGVDDGT ESDTSVTATS RKSSQIPKRN GKENGTENLK 2750
IDRPEDAGEK EHVIKSAVGH KNEPKLDNCH SVSRVKAQGQ DSLEAQLSSL 2800
ESSRRVHTST PSDKNLLDTY NAELLKSDSD NNNSDDCGNI LPSDIMDFVL 2850
KNTPSMQALG ESPESSSSEL LTLGEGLGLD SNREKDIGLF EVFSQQLPAT 2900
EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ NPSRLAVISD 2950
SGEKRVTITE KSVASSEGDP ALLSPGVDPA PEGHMTPDHF IQGHMDADHI 3000
SSPPCGSVEQ GHGNSQDLTR NSGTPGLQVP VSPTVPVQNQ KYVPSSTDSP 3050
GPSQISNAAV QTTPPHLKPA TEKLIVVNQN MQPLYVLQTL PNGVTQKIQL 3100
TSPVSSTPSV METNTSVLGP MGSGLTLTTG LNPSLPPSPS LFPPASKGLL 3150
SVPHHQHLHS FPAAAQSSFP PNISSPPSGL LIGVQPPPDP QLLGSEANQR 3200
TDLTTTVATP SSGLKKRPIS RLHTRKNKKL APSSAPSNIA PSDVVSNMTL 3250
INFTPSQLSN HPSLLDLGSL NPSSHRTVPN IIKRSKSGIM YFEQAPLLPP 3300
QSVGGTAATA AGSSTISQDT SHLTSGPVSA LASGSSVLNV VSMQTTAAPT 3350
SSTSVPGHVT LANQRLLGTP DIGSISHLLI KASHQSLGIQ DQPVALPPSS 3400
GMFPQLGTSQ TPSAAAMTAA SSICVLPSSQ TAGMTAASPP GEAEEHYKLQ 3450
RGNQLLAGKT GTLTSQRDRD PDSAPGTQPS NFTQTAEAPN GVRLEQNKTL 3500
PSAKPASSAS PGSSPSSGQQ SGSSSVPGPT KPKPKAKRIQ LPLDKGSGKK 3550
HKVSHLRTSS EAHIPHRDTD PAPQPSVTRT PRANREQQDA AGVEQPSQKE 3600
CGQPAGPVAA LPEVQATQNP ANEQENAEPK AMEEEESGFS SPLMLWLQQE 3650
QKRKESITER KPKKGLVFEI SSDDGFQICA ESIEDAWKSL TDKVQEARSN 3700
ARLKQLSFAG VNGLRMLGIL HDAVVFLIEQ LAGAKHCRNY KFRFHKPEEA 3750
NEPPLNPHGS ARAEVHLRQS AFDMFNFLAS KHRQPPEYNP NDEEEEEVQL 3800
KSARRATSMD LPMPMRFRHL KKTSKEAVGV YRSPIHGRGL FCKRNIDAGE 3850
MVIEYAGNVI RSIQTDKREK YYDSKGIGCY MFRIDDSEVV DATMHGNAAR 3900
FINHSCEPNC YSRVINIDGQ KHIVIFAMRK IYRGEELTYD YKFPIEDASN 3950
KLPCNCGAKK CRKFLN 3966
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.

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. VSP_006667

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti372 – 3721Q → E in BAE28820. 1 Publication
Sequence conflicti554 – 5541Q → K in AAA62593. 1 Publication
Sequence conflicti564 – 5641L → F in AAA62593. 1 Publication
Sequence conflicti797 – 7971P → S in BAE28820. 1 Publication
Sequence conflicti806 – 8061E → D in AAA62593. 1 Publication
Sequence conflicti806 – 8061E → D in BAE28820. 1 Publication
Sequence conflicti821 – 8211L → P in AAA62593. 1 Publication
Sequence conflicti821 – 8211L → P in BAE28820. 1 Publication
Sequence conflicti1069 – 10691C → Y in AAA62593. 1 Publication
Sequence conflicti1230 – 12301A → S in AAA62593. 1 Publication
Sequence conflicti1349 – 13491R → L in AAA62593. 1 Publication
Sequence conflicti1437 – 14371A → S in AAA62593. 1 Publication
Sequence conflicti1440 – 14401G → E in AAA62593. 1 Publication
Sequence conflicti1632 – 16321A → P in AAA62593. 1 Publication
Sequence conflicti2292 – 22921S → L in AAA62593. 1 Publication
Sequence conflicti3481 – 34811N → I in AAA62593. 1 Publication
Sequence conflicti3493 – 34931R → S in AAA62593. 1 Publication
Sequence conflicti3548 – 35481G → V in AAA62593. 1 Publication
Sequence conflicti3769 – 37691Q → K in AAA62593. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS40603.1. [P55200-2 ]
RefSeqi NP_001074518.1. NM_001081049.1. [P55200-2 ]
UniGenei Mm.2389.

3D structure databases

ProteinModelPortali P55200.
SMRi P55200. Positions 6-39, 101-133, 1144-1200, 1563-1781, 2836-2865, 3787-3966.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-58597N.
IntActi P55200. 1 interaction.
MINTi MINT-4084570.

PTM databases

PhosphoSitei P55200.

Proteomic databases

PaxDbi P55200.
PRIDEi P55200.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000002095 ; ENSMUSP00000002095 ; ENSMUSG00000002028 . [P55200-2 ]
ENSMUST00000114689 ; ENSMUSP00000110337 ; ENSMUSG00000002028 . [P55200-1 ]
GeneIDi 214162.
KEGGi mmu:214162.
UCSCi uc009pep.1. mouse. [P55200-2 ]
uc009peq.1. mouse. [P55200-1 ]

Organism-specific databases

CTDi 4297.
MGIi MGI:96995. Kmt2a.

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00740000115089.
HOGENOMi HOG000112954.
HOVERGENi HBG051927.
InParanoidi P55200.
KOi K09186.
OMAi RIMSPMR.
OrthoDBi EOG7XH6NX.
TreeFami TF319820.

Miscellaneous databases

NextBioi 374214.
PROi P55200.
SOURCEi Search...

Gene expression databases

ArrayExpressi P55200.
Bgeei P55200.
CleanExi MM_MLL1.
Genevestigatori P55200.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
InterProi IPR017956. 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 ]
Pfami PF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view ]
PIRSFi PIRSF010354. Methyltransferase_trithorax. 1 hit.
SMARTi SM00384. 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 ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEi PS50014. 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 ]
ProtoNeti Search...

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. "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.

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: July 9, 2014
This is version 134 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

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