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O14686 (KMT2D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=Lysine N-methyltransferase 2D
EC=2.1.1.43
Alternative name(s):
ALL1-related protein
Myeloid/lymphoid or mixed-lineage leukemia protein 2
Gene names
Name:KMT2D
Synonyms:ALR, MLL2, MLL4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length5537 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone methyltransferase. Methylates 'Lys-4' of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. Ref.5 Ref.7 Ref.8

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.5 Ref.7

Subunit structure

Component of the MLL2/3 complex (also named ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. Interacts with ESR1; interaction is direct. Ref.3 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10

Subcellular location

Nucleus Probable.

Tissue specificity

Expressed in most adult tissues, including a variety of hematoipoietic cells, with the exception of the liver.

Domain

LXXLL motifs 5 and 6 are essential for the association with ESR1 nuclear receptor.

Involvement in disease

Kabuki syndrome 1 (KABUK1) [MIM:147920]: A congenital mental retardation syndrome with additional features, including postnatal dwarfism, a peculiar facies characterized by long palpebral fissures with eversion of the lateral third of the lower eyelids, a broad and depressed nasal tip, large prominent earlobes, a cleft or high-arched palate, scoliosis, short fifth finger, persistence of fingerpads, radiographic abnormalities of the vertebrae, hands, and hip joints, and recurrent otitis media in infancy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19

Miscellaneous

This gene mapped to a chromosomal region involved in duplications and translocations associated with cancer.

Sequence similarities

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

Contains 1 FYR C-terminal domain.

Contains 1 FYR N-terminal domain.

Contains 5 PHD-type zinc fingers.

Contains 1 post-SET domain.

Contains 4 RING-type zinc fingers.

Contains 1 SET domain.

Caution

Another protein KMT2B/MLL4, located on chromosome 19, was first named MLL2 (see AC Q9UMN6). Thus, KMT2B/MLL4 is often referred to as MLL2 and vice versa in the literature.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin silencing

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3-K4 methylation

Inferred from sequence or structural similarity PubMed 17178841. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

oocyte growth

Inferred from sequence or structural similarity. Source: UniProtKB

oogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of intracellular estrogen receptor signaling pathway

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.5. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

response to estrogen

Inferred from direct assay Ref.5. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthistone methyltransferase complex

Inferred from physical interaction PubMed 14992727. Source: MGI

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionDNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

histone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction Ref.3Ref.5Ref.6PubMed 17178841. Source: IntAct

transcription regulatory region DNA binding

Inferred from direct assay Ref.5. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ESR1P033723EBI-996065,EBI-78473
NCOA6Q146866EBI-996065,EBI-78670

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14686-1)

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 3 (identifier: O14686-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1729-1729: E → EGET

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 55375537Histone-lysine N-methyltransferase 2D
PRO_0000124878

Regions

Repeat442 – 44651
Repeat460 – 46452
Repeat469 – 47353
Repeat496 – 50054
Repeat504 – 50855
Repeat521 – 52556
Repeat555 – 55957
Repeat564 – 56858
Repeat573 – 57759
Repeat582 – 586510
Repeat609 – 613511
Repeat618 – 622512
Repeat627 – 631513
Repeat645 – 649514
Repeat663 – 667515
Domain5175 – 523561FYR N-terminal
Domain5236 – 532186FYR C-terminal
Domain5397 – 5513117SET
Domain5521 – 553717Post-SET
Zinc finger226 – 27651PHD-type 1
Zinc finger229 – 27446RING-type 1; atypical
Zinc finger273 – 32351PHD-type 2
Zinc finger276 – 32146RING-type 2; degenerate
Zinc finger1377 – 143054PHD-type 3
Zinc finger1427 – 147751PHD-type 4
Zinc finger1504 – 155956PHD-type 5
Zinc finger1507 – 155751RING-type 3; atypical
Zinc finger5092 – 513746RING-type 4; degenerate
Region439 – 66823015 X 5 AA repeats of S/P-P-P-E/P-E/A
Region5474 – 54752S-adenosyl-L-methionine binding By similarity
Coiled coil2669 – 270739 Potential
Coiled coil3249 – 328234 Potential
Coiled coil3562 – 361453 Potential
Coiled coil3714 – 375037 Potential
Coiled coil3897 – 397579 Potential
Motif2686 – 26905LXXLL motif 1
Motif3038 – 30425LXXLL motif 2
Motif4222 – 423615LXXLL motif 3
Motif4253 – 42575LXXLL motif 4
Motif4463 – 44675LXXLL motif 5
Motif4990 – 49945LXXLL motif 6
Compositional bias229 – 32698Cys-rich
Compositional bias374 – 1197824Pro-rich
Compositional bias1290 – 132839Arg-rich
Compositional bias1351 – 13555Poly-Glu
Compositional bias1397 – 1510114Cys-rich
Compositional bias2107 – 2626520Pro-rich
Compositional bias2385 – 23928Poly-Pro
Compositional bias2707 – 27137Poly-Ala
Compositional bias2811 – 282212Gln-rich
Compositional bias2862 – 2978117Pro-rich
Compositional bias3261 – 42751015Gln-rich
Compositional bias4241 – 4360120Pro-rich
Compositional bias4909 – 497769Pro-rich
Compositional bias5494 – 54974Poly-Ile

Sites

Metal binding54771Zinc By similarity
Metal binding55251Zinc By similarity
Metal binding55271Zinc By similarity
Metal binding55321Zinc By similarity
Binding site54511S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue271Phosphoserine Ref.12
Modified residue16061Phosphoserine Ref.16
Modified residue16711Phosphoserine Ref.14 Ref.17
Modified residue22461N6-acetyllysine Ref.15
Modified residue22741Phosphoserine Ref.12 Ref.14 Ref.17
Modified residue23091Phosphoserine Ref.12
Modified residue23111Phosphoserine Ref.12
Modified residue30791N6-acetyllysine Ref.15
Modified residue31301Phosphoserine Ref.4
Modified residue31971Phosphothreonine Ref.12 Ref.14 Ref.16
Modified residue31991Phosphoserine Ref.16
Modified residue34331N6-acetyllysine Ref.15
Modified residue42151Phosphoserine Ref.16
Modified residue43591Phosphoserine Ref.14 Ref.16
Modified residue44651N6-acetyllysine Ref.15
Modified residue47381Phosphoserine Ref.11 Ref.16 Ref.17
Modified residue47761N6-acetyllysine Ref.15
Modified residue48221Phosphoserine Ref.12 Ref.14

Natural variations

Alternative sequence17291E → EGET in isoform 3.
VSP_008560
Natural variant4761A → T.
Corresponds to variant rs1064210 [ dbSNP | Ensembl ].
VAR_057359
Natural variant6921P → T. Ref.18
Corresponds to variant rs202076833 [ dbSNP | Ensembl ].
VAR_064370
Natural variant8131P → L. Ref.18
Corresponds to variant rs75226229 [ dbSNP | Ensembl ].
VAR_064371
Natural variant23821P → S. Ref.18
Corresponds to variant rs3741626 [ dbSNP | Ensembl ].
VAR_064372
Natural variant24601R → C. Ref.18
VAR_064373
Natural variant25571P → L. Ref.18
Corresponds to variant rs189888707 [ dbSNP | Ensembl ].
VAR_064374
Natural variant33981M → V. Ref.18
Corresponds to variant rs75937132 [ dbSNP | Ensembl ].
VAR_064375
Natural variant34191D → G. Ref.18
Corresponds to variant rs146044282 [ dbSNP | Ensembl ].
VAR_064376
Natural variant43571R → S. Ref.18
VAR_064377
Natural variant51091C → F in KABUK1. Ref.19
VAR_063830
Natural variant51791R → H in KABUK1. Ref.19
VAR_063831
Natural variant52101Y → C in KABUK1. Ref.18
VAR_064378
Natural variant52141R → H in KABUK1. Ref.19
VAR_063832
Natural variant52241R → H.
Corresponds to variant rs3782356 [ dbSNP | Ensembl ].
VAR_017115
Natural variant53401R → L in KABUK1. Ref.19
VAR_063833
Natural variant54281G → D in KABUK1. Ref.18
VAR_064379
Natural variant54641T → M in KABUK1. Ref.19
VAR_063834

Experimental info

Sequence conflict51K → N in AAC51734. Ref.1
Sequence conflict141E → Q in AAC51734. Ref.1
Sequence conflict751S → A in AAC51734. Ref.1
Sequence conflict1561E → Q in AAC51734. Ref.1
Sequence conflict674 – 948275Missing in AAC51734. Ref.1
Sequence conflict11781Q → R in AAC51734. Ref.1
Sequence conflict11781Q → R in AAC51735. Ref.1
Sequence conflict1544 – 15474EQAA → DHAP in AAC51734. Ref.1
Sequence conflict1544 – 15474EQAA → DHAP in AAC51735. Ref.1
Sequence conflict17611K → R in AAC51734. Ref.1
Sequence conflict17611K → R in AAC51735. Ref.1
Sequence conflict17661D → G in AAC51734. Ref.1
Sequence conflict17661D → G in AAC51735. Ref.1
Sequence conflict21711V → A in AAC51734. Ref.1
Sequence conflict21711V → A in AAC51735. Ref.1
Sequence conflict24131A → V in AAC51734. Ref.1
Sequence conflict24131A → V in AAC51735. Ref.1
Sequence conflict30791K → E in AAC51734. Ref.1
Sequence conflict30791K → E in AAC51735. Ref.1
Sequence conflict32871S → P in AAC51734. Ref.1
Sequence conflict32871S → P in AAC51735. Ref.1
Sequence conflict33191G → V in AAC51734. Ref.1
Sequence conflict33191G → V in AAC51735. Ref.1
Sequence conflict34221D → G in AAC51734. Ref.1
Sequence conflict34221D → G in AAC51735. Ref.1
Sequence conflict44781R → Q in AAC51734. Ref.1
Sequence conflict44781R → Q in AAC51735. Ref.1
Sequence conflict47471A → D in AAC51734. Ref.1
Sequence conflict47471A → D in AAC51735. Ref.1
Sequence conflict47931A → D in AAC51734. Ref.1
Sequence conflict47931A → D in AAC51735. Ref.1
Sequence conflict48261A → G in AAC51734. Ref.1
Sequence conflict48261A → G in AAC51735. Ref.1
Sequence conflict48651P → A in AAC51734. Ref.1
Sequence conflict48651P → A in AAC51735. Ref.1
Sequence conflict48711S → R in AAC51734. Ref.1
Sequence conflict48711S → R in AAC51735. Ref.1
Sequence conflict48931S → R in AAC51734. Ref.1
Sequence conflict48931S → R in AAC51735. Ref.1
Sequence conflict49741S → T in AAC51734. Ref.1
Sequence conflict49741S → T in AAC51735. Ref.1
Sequence conflict51161A → G in AAC51734. Ref.1
Sequence conflict51161A → G in AAC51735. Ref.1
Sequence conflict55221K → E in AAC51734. Ref.1
Sequence conflict55221K → E in AAC51735. Ref.1

Secondary structure

... 5537
Helix Strand Turn

Details...

Sequences

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

Last modified November 30, 2010. Version 2.
Checksum: 31C6DAB0A754F72A

FASTA5,537593,389
        10         20         30         40         50         60 
MDSQKLAGED KDSEPAADGP AASEDPSATE SDLPNPHVGE VSVLSSGSPR LQETPQDCSG 

        70         80         90        100        110        120 
GPVRRCALCN CGEPSLHGQR ELRRFELPFD WPRCPVVSPG GSPGPNEAVL PSEDLSQIGF 

       130        140        150        160        170        180 
PEGLTPAHLG EPGGSCWAHH WCAAWSAGVW GQEGPELCGV DKAIFSGISQ RCSHCTRLGA 

       190        200        210        220        230        240 
SIPCRSPGCP RLYHFPCATA SGSFLSMKTL QLLCPEHSEG AAYLEEARCA VCEGPGELCD 

       250        260        270        280        290        300 
LFFCTSCGHH YHGACLDTAL TARKRAGWQC PECKVCQACR KPGNDSKMLV CETCDKGYHT 

       310        320        330        340        350        360 
FCLKPPMEEL PAHSWKCKAC RVCRACGAGS AELNPNSEWF ENYSLCHRCH KAQGGQTIRS 

       370        380        390        400        410        420 
VAEQHTPVCS RFSPPEPGDT PTDEPDALYV ACQGQPKGGH VTSMQPKEPG PLQCEAKPLG 

       430        440        450        460        470        480 
KAGVQLEPQL EAPLNEEMPL LPPPEESPLS PPPEESPTSP PPEASRLSPP PEELPASPLP 

       490        500        510        520        530        540 
EALHLSRPLE ESPLSPPPEE SPLSPPPESS PFSPLEESPL SPPEESPPSP ALETPLSPPP 

       550        560        570        580        590        600 
EASPLSPPFE ESPLSPPPEE LPTSPPPEAS RLSPPPEESP MSPPPEESPM SPPPEASRLF 

       610        620        630        640        650        660 
PPFEESPLSP PPEESPLSPP PEASRLSPPP EDSPMSPPPE ESPMSPPPEV SRLSPLPVVS 

       670        680        690        700        710        720 
RLSPPPEESP LSPPPEESPT SPPPEASRLS PPPEDSPTSP PPEDSPASPP PEDSLMSLPL 

       730        740        750        760        770        780 
EESPLLPLPE EPQLCPRSEG PHLSPRPEEP HLSPRPEEPH LSPQAEEPHL SPQPEEPCLC 

       790        800        810        820        830        840 
AVPEEPHLSP QAEGPHLSPQ PEELHLSPQT EEPHLSPVPE EPCLSPQPEE SHLSPQSEEP 

       850        860        870        880        890        900 
CLSPRPEESH LSPELEKPPL SPRPEKPPEE PGQCPAPEEL PLFPPPGEPS LSPLLGEPAL 

       910        920        930        940        950        960 
SEPGEPPLSP LPEELPLSPS GEPSLSPQLM PPDPLPPPLS PIITAAAPPA LSPLGELEYP 

       970        980        990       1000       1010       1020 
FGAKGDSDPE SPLAAPILET PISPPPEANC TDPEPVPPMI LPPSPGSPVG PASPILMEPL 

      1030       1040       1050       1060       1070       1080 
PPQCSPLLQH SLVPQNSPPS QCSPPALPLS VPSPLSPIGK VVGVSDEAEL HEMETEKVSE 

      1090       1100       1110       1120       1130       1140 
PECPALEPSA TSPLPSPMGD LSCPAPSPAP ALDDFSGLGE DTAPLDGIDA PGSQPEPGQT 

      1150       1160       1170       1180       1190       1200 
PGSLASELKG SPVLLDPEEL APVTPMEVYP ECKQTAGQGS PCEEQEEPRA PVAPTPPTLI 

      1210       1220       1230       1240       1250       1260 
KSDIVNEISN LSQGDASASF PGSEPLLGSP DPEGGGSLSM ELGVSTDVSP ARDEGSLRLC 

      1270       1280       1290       1300       1310       1320 
TDSLPETDDS LLCDAGTAIS GGKAEGEKGR RRSSPARSRI KQGRSSSFPG RRRPRGGAHG 

      1330       1340       1350       1360       1370       1380 
GRGRGRARLK STASSIETLV VADIDSSPSK EEEEEDDDTM QNTVVLFSNT DKFVLMQDMC 

      1390       1400       1410       1420       1430       1440 
VVCGSFGRGA EGHLLACSQC SQCYHPYCVN SKITKVMLLK GWRCVECIVC EVCGQASDPS 

      1450       1460       1470       1480       1490       1500 
RLLLCDDCDI SYHTYCLDPP LLTVPKGGWK CKWCVSCMQC GAASPGFHCE WQNSYTHCGP 

      1510       1520       1530       1540       1550       1560 
CASLVTCPIC HAPYVEEDLL IQCRHCERWM HAGCESLFTE DDVEQAADEG FDCVSCQPYV 

      1570       1580       1590       1600       1610       1620 
VKPVAPVAPP ELVPMKVKEP EPQYFRFEGV WLTETGMALL RNLTMSPLHK RRQRRGRLGL 

      1630       1640       1650       1660       1670       1680 
PGEAGLEGSE PSDALGPDDK KDGDLDTDEL LKGEGGVEHM ECEIKLEGPV SPDVEPGKEE 

      1690       1700       1710       1720       1730       1740 
TEESKKRKRK PYRPGIGGFM VRQRKSHTRT KKGPAAQAEV LSGDGQPDEV IPADLPAEGA 

      1750       1760       1770       1780       1790       1800 
VEQSLAEGDE KKKQQRRGRK KSKLEDMFPA YLQEAFFGKE LLDLSRKALF AVGVGRPSFG 

      1810       1820       1830       1840       1850       1860 
LGTPKAKGDG GSERKELPTS QKGDDGPDIA DEESRGLEGK ADTPGPEDGG VKASPVPSDP 

      1870       1880       1890       1900       1910       1920 
EKPGTPGEGM LSSDLDRIST EELPKMESKD LQQLFKDVLG SEREQHLGCG TPGLEGSRTP 

      1930       1940       1950       1960       1970       1980 
LQRPFLQGGL PLGNLPSSSP MDSYPGLCQS PFLDSRERGG FFSPEPGEPD SPWTGSGGTT 

      1990       2000       2010       2020       2030       2040 
PSTPTTPTTE GEGDGLSYNQ RSLQRWEKDE ELGQLSTISP VLYANINFPN LKQDYPDWSS 

      2050       2060       2070       2080       2090       2100 
RCKQIMKLWR KVPAADKAPY LQKAKDNRAA HRINKVQKQA ESQINKQTKV GDIARKTDRP 

      2110       2120       2130       2140       2150       2160 
ALHLRIPPQP GALGSPPPAA APTIFIGSPT TPAGLSTSAD GFLKPPAGSV PGPDSPGELF 

      2170       2180       2190       2200       2210       2220 
LKLPPQVPAQ VPSQDPFGLA PAYPLEPRFP TAPPTYPPYP SPTGAPAQPP MLGASSRPGA 

      2230       2240       2250       2260       2270       2280 
GQPGEFHTTP PGTPRHQPST PDPFLKPRCP SLDNLAVPES PGVGGGKASE PLLSPPPFGE 

      2290       2300       2310       2320       2330       2340 
SRKALEVKKE ELGASSPSYG PPNLGFVDSP SSGTHLGGLE LKTPDVFKAP LTPRASQVEP 

      2350       2360       2370       2380       2390       2400 
QSPGLGLRPQ EPPPAQALAP SPPSHPDIFR PGSYTDPYAQ PPLTPRPQPP PPESCCALPP 

      2410       2420       2430       2440       2450       2460 
RSLPSDPFSR VPASPQSQSS SQSPLTPRPL SAEAFCPSPV TPRFQSPDPY SRPPSRPQSR 

      2470       2480       2490       2500       2510       2520 
DPFAPLHKPP RPQPPEVAFK AGSLAHTSLG AGGFPAALPA GPAGELHAKV PSGQPPNFVR 

      2530       2540       2550       2560       2570       2580 
SPGTGAFVGT PSPMRFTFPQ AVGEPSLKPP VPQPGLPPPH GINSHFGPGP TLGKPQSTNY 

      2590       2600       2610       2620       2630       2640 
TVATGNFHPS GSPLGPSSGS TGESYGLSPL RPPSVLPPPA PDGSLPYLSH GASQRSGITS 

      2650       2660       2670       2680       2690       2700 
PVEKREDPGT GMGSSLATAE LPGTQDPGMS GLSQTELEKQ RQRQRLRELL IRQQIQRNTL 

      2710       2720       2730       2740       2750       2760 
RQEKETAAAA AGAVGPPGSW GAEPSSPAFE QLSRGQTPFA GTQDKSSLVG LPPSKLSGPI 

      2770       2780       2790       2800       2810       2820 
LGPGSFPSDD RLSRPPPPAT PSSMDVNSRQ LVGGSQAFYQ RAPYPGSLPL QQQQQQLWQQ 

      2830       2840       2850       2860       2870       2880 
QQATAATSMR FAMSARFPST PGPELGRQAL GSPLAGISTR LPGPGEPVPG PAGPAQFIEL 

      2890       2900       2910       2920       2930       2940 
RHNVQKGLGP GGTPFPGQGP PQRPRFYPVS EDPHRLAPEG LRGLAVSGLP PQKPSAPPAP 

      2950       2960       2970       2980       2990       3000 
ELNNSLHPTP HTKGPTLPTG LELVNRPPSS TELGRPNPLA LEAGKLPCED PELDDDFDAH 

      3010       3020       3030       3040       3050       3060 
KALEDDEELA HLGLGVDVAK GDDELGTLEN LETNDPHLDD LLNGDEFDLL AYTDPELDTG 

      3070       3080       3090       3100       3110       3120 
DKKDIFNEHL RLVESANEKA EREALLRGVE PGPLGPEERP PPAADASEPR LASVLPEVKP 

      3130       3140       3150       3160       3170       3180 
KVEEGGRHPS PCQFTIATPK VEPAPAANSL GLGLKPGQSM MGSRDTRMGT GPFSSSGHTA 

      3190       3200       3210       3220       3230       3240 
EKASFGATGG PPAHLLTPSP LSGPGGSSLL EKFELESGAL TLPGGPAASG DELDKMESSL 

      3250       3260       3270       3280       3290       3300 
VASELPLLIE DLLEHEKKEL QKKQQLSAQL QPAQQQQQQQ QQHSLLSAPG PAQAMSLPHE 

      3310       3320       3330       3340       3350       3360 
GSSPSLAGSQ QQLSLGLAGA RQPGLPQPLM PTQPPAHALQ QRLAPSMAMV SNQGHMLSGQ 

      3370       3380       3390       3400       3410       3420 
HGGQAGLVPQ QSSQPVLSQK PMGTMPPSMC MKPQQLAMQQ QLANSFFPDT DLDKFAAEDI 

      3430       3440       3450       3460       3470       3480 
IDPIAKAKMV ALKGIKKVMA QGSIGVAPGM NRQQVSLLAQ RLSGGPSSDL QNHVAAGSGQ 

      3490       3500       3510       3520       3530       3540 
ERSAGDPSQP RPNPPTFAQG VINEADQRQY EEWLFHTQQL LQMQLKVLEE QIGVHRKSRK 

      3550       3560       3570       3580       3590       3600 
ALCAKQRTAK KAGREFPEAD AEKLKLVTEQ QSKIQKQLDQ VRKQQKEHTN LMAEYRNKQQ 

      3610       3620       3630       3640       3650       3660 
QQQQQQQQQQ QQHSAVLALS PSQSPRLLTK LPGQLLPGHG LQPPQGPPGG QAGGLRLTPG 

      3670       3680       3690       3700       3710       3720 
GMALPGQPGG PFLNTALAQQ QQQQHSGGAG SLAGPSGGFF PGNLALRSLG PDSRLLQERQ 

      3730       3740       3750       3760       3770       3780 
LQLQQQRMQL AQKLQQQQQQ QQQQQHLLGQ VAIQQQQQQG PGVQTNQALG PKPQGLMPPS 

      3790       3800       3810       3820       3830       3840 
SHQGLLVQQL SPQPPQGPQG MLGPAQVAVL QQQHPGALGP QGPHRQVLMT QSRVLSSPQL 

      3850       3860       3870       3880       3890       3900 
AQQGQGLMGH RLVTAQQQQQ QQQHQQQGSM AGLSHLQQSL MSHSGQPKLS AQPMGSLQQL 

      3910       3920       3930       3940       3950       3960 
QQQQQLQQQQ QLQQQQQQQL QQQQQLQQQQ LQQQQQQQQL QQQQQQQLQQ QQQQLQQQQQ 

      3970       3980       3990       4000       4010       4020 
QQQQQFQQQQ QQQQMGLLNQ SRTLLSPQQQ QQQQVALGPG MPAKPLQHFS SPGALGPTLL 

      4030       4040       4050       4060       4070       4080 
LTGKEQNTVD PAVSSEATEG PSTHQGGPLA IGTTPESMAT EPGEVKPSLS GDSQLLLVQP 

      4090       4100       4110       4120       4130       4140 
QPQPQPSSLQ LQPPLRLPGQ QQQQVSLLHT AGGGSHGQLG SGSSSEASSV PHLLAQPSVS 

      4150       4160       4170       4180       4190       4200 
LGDQPGSMTQ NLLGPQQPML ERPMQNNTGP QPPKPGPVLQ SGQGLPGVGI MPTVGQLRAQ 

      4210       4220       4230       4240       4250       4260 
LQGVLAKNPQ LRHLSPQQQQ QLQALLMQRQ LQQSQAVRQT PPYQEPGTQT SPLQGLLGCQ 

      4270       4280       4290       4300       4310       4320 
PQLGGFPGPQ TGPLQELGAG PRPQGPPRLP APPGALSTGP VLGPVHPTPP PSSPQEPKRP 

      4330       4340       4350       4360       4370       4380 
SQLPSPSSQL PTEAQLPPTH PGTPKPQGPT LEPPPGRVSP AAAQLADTLF SKGLGPWDPP 

      4390       4400       4410       4420       4430       4440 
DNLAETQKPE QSSLVPGHLD QVNGQVVPEA SQLSIKQEPR EEPCALGAQS VKREANGEPI 

      4450       4460       4470       4480       4490       4500 
GAPGTSNHLL LAGPRSEAGH LLLQKLLRAK NVQLSTGRGS EGLRAEINGH IDSKLAGLEQ 

      4510       4520       4530       4540       4550       4560 
KLQGTPSNKE DAAARKPLTP KPKRVQKASD RLVSSRKKLR KEDGVRASEA LLKQLKQELS 

      4570       4580       4590       4600       4610       4620 
LLPLTEPAIT ANFSLFAPFG SGCPVNGQSQ LRGAFGSGAL PTGPDYYSQL LTKNNLSNPP 

      4630       4640       4650       4660       4670       4680 
TPPSSLPPTP PPSVQQKMVN GVTPSEELGE HPKDAASARD SERALRDTSE VKSLDLLAAL 

      4690       4700       4710       4720       4730       4740 
PTPPHNQTED VRMESDEDSD SPDSIVPASS PESILGEEAP RFPHLGSGRW EQEDRALSPV 

      4750       4760       4770       4780       4790       4800 
IPLIPRASIP VFPDTKPYGA LGLEVPGKLP VTTWEKGKGS EVSVMLTVSA AAAKNLNGVM 

      4810       4820       4830       4840       4850       4860 
VAVAELLSMK IPNSYEVLFP ESPARAGTEP KKGEAEGPGG KEKGLEGKSP DTGPDWLKQF 

      4870       4880       4890       4900       4910       4920 
DAVLPGYTLK SQLDILSLLK QESPAPEPPT QHSYTYNVSN LDVRQLSAPP PEEPSPPPSP 

      4930       4940       4950       4960       4970       4980 
LAPSPASPPT EPLVELPTEP LAEPPVPSPL PLASSPESAR PKPRARPPEE GEDSRPPRLK 

      4990       5000       5010       5020       5030       5040 
KWKGVRWKRL RLLLTIQKGS GRQEDEREVA EFMEQLGTAL RPDKVPRDMR RCCFCHEEGD 

      5050       5060       5070       5080       5090       5100 
GATDGPARLL NLDLDLWVHL NCALWSTEVY ETQGGALMNV EVALHRGLLT KCSLCQRTGA 

      5110       5120       5130       5140       5150       5160 
TSSCNRMRCP NVYHFACAIR AKCMFFKDKT MLCPMHKIKG PCEQELSSFA VFRRVYIERD 

      5170       5180       5190       5200       5210       5220 
EVKQIASIIQ RGERLHMFRV GGLVFHAIGQ LLPHQMADFH SATALYPVGY EATRIYWSLR 

      5230       5240       5250       5260       5270       5280 
TNNRRCCYRC SIGENNGRPE FVIKVIEQGL EDLVFTDASP QAVWNRIIEP VAAMRKEADM 

      5290       5300       5310       5320       5330       5340 
LRLFPEYLKG EELFGLTVHA VLRIAESLPG VESCQNYLFR YGRHPLMELP LMINPTGCAR 

      5350       5360       5370       5380       5390       5400 
SEPKILTHYK RPHTLNSTSM SKAYQSTFTG ETNTPYSKQF VHSKSSQYRR LRTEWKNNVY 

      5410       5420       5430       5440       5450       5460 
LARSRIQGLG LYAAKDLEKH TMVIEYIGTI IRNEVANRRE KIYEEQNRGI YMFRINNEHV 

      5470       5480       5490       5500       5510       5520 
IDATLTGGPA RYINHSCAPN CVAEVVTFDK EDKIIIISSR RIPKGEELTY DYQFDFEDDQ 

      5530 
HKIPCHCGAW NCRKWMN 

« Hide

Isoform 3 [UniParc].

Checksum: BB9AC95AA8BC0DD4
Show »

FASTA5,540593,677

References

« Hide 'large scale' references
[1]"Structure and expression pattern of human ALR, a novel gene with strong homology to ALL-1 involved in acute leukemia and to Drosophila trithorax."
Prasad R., Zhadanov A.B., Sedkov Y., Bullrich F., Druck T., Rallapalli R., Yano T., Alder H., Croce C.M., Huebner K., Mazo A., Canaani E.
Oncogene 15:549-560(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins."
Goo Y.-H., Sohn Y.C., Kim D.-H., Kim S.-W., Kang M.-J., Jung D.-J., Kwak E., Barlev N.A., Berger S.L., Chow V.T., Roeder R.G., Azorsa D.O., Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C., Lee J.W.
Mol. Cell. Biol. 23:140-149(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MLL2/3 COMPLEX.
Tissue: Cervix carcinoma.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Identification of the MLL2 complex as a coactivator for estrogen receptor alpha."
Mo R., Rao S.M., Zhu Y.-J.
J. Biol. Chem. 281:15714-15720(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, IDENTIFICATION IN THE MLL2 COMPLEX, LXXLL MOTIFS, INTERACTION WITH ESR1.
[6]"Coactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferases."
Lee S., Lee D.K., Dou Y., Lee J., Lee B., Kwak E., Kong Y.Y., Lee S.K., Roeder R.G., Lee J.W.
Proc. Natl. Acad. Sci. U.S.A. 103:15392-15397(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
[7]"PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K.
J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
[8]"A histone H3 lysine 27 demethylase regulates animal posterior development."
Lan F., Bayliss P.E., Rinn J.L., Whetstine J.R., Wang J.K., Chen S., Iwase S., Alpatov R., Issaeva I., Canaani E., Roberts T.M., Chang H.Y., Shi Y.
Nature 449:689-694(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE MLL2/3 COMPLEX.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination."
Lee M.G., Villa R., Trojer P., Norman J., Yan K.P., Reinberg D., Di Croce L., Shiekhattar R.
Science 318:447-450(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MLL2/3 COMPLEX.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-2274; SER-2309; SER-2311; THR-3197 AND SER-4822, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1671; SER-2274; THR-3197; SER-4359 AND SER-4822, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2246; LYS-3079; LYS-3433; LYS-4465 AND LYS-4776, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1606; THR-3197; SER-3199; SER-4215; SER-4359 AND SER-4738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1671; SER-2274 AND SER-4738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"MLL2 mutation spectrum in 45 patients with Kabuki syndrome."
Paulussen A.D., Stegmann A.P., Blok M.J., Tserpelis D., Posma-Velter C., Detisch Y., Smeets E.E., Wagemans A., Schrander J.J., van den Boogaard M.J., van der Smagt J., van Haeringen A., Stolte-Dijkstra I., Kerstjens-Frederikse W.S., Mancini G.M., Wessels M.W., Hennekam R.C., Vreeburg M. expand/collapse author list , Geraedts J., de Ravel T., Fryns J.P., Smeets H.J., Devriendt K., Schrander-Stumpel C.T.
Hum. Mutat. 32:E2018-E2025(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS KABUK1 CYS-5210 AND ASP-5428, VARIANTS THR-692; LEU-813; SER-2382; CYS-2460; LEU-2557; VAL-3398; GLY-3419 AND SER-4357.
[19]"Exome sequencing identifies MLL2 mutations as a cause of Kabuki syndrome."
Ng S.B., Bigham A.W., Buckingham K.J., Hannibal M.C., McMillin M.J., Gildersleeve H.I., Beck A.E., Tabor H.K., Cooper G.M., Mefford H.C., Lee C., Turner E.H., Smith J.D., Rieder M.J., Yoshiura K., Matsumoto N., Ohta T., Niikawa N. expand/collapse author list , Nickerson D.A., Bamshad M.J., Shendure J.
Nat. Genet. 42:790-793(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS KABUK1 PHE-5109; HIS-5179; HIS-5214; LEU-5340 AND MET-5464.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF010403 mRNA. Translation: AAC51734.1.
AF010404 mRNA. Translation: AAC51735.1.
AC011603 Genomic DNA. No translation available.
CCDSCCDS44873.1. [O14686-1]
PIRT03454.
T03455.
RefSeqNP_003473.3. NM_003482.3. [O14686-1]
XP_005269219.1. XM_005269162.2. [O14686-1]
XP_006719677.1. XM_006719614.1. [O14686-3]
UniGeneHs.731384.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UVKX-ray1.40B5337-5347[»]
4ERQX-ray1.91D/E/F5333-5346[»]
ProteinModelPortalO14686.
SMRO14686. Positions 220-323, 2000-2077.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113758. 25 interactions.
DIPDIP-37875N.
IntActO14686. 16 interactions.
MINTMINT-1192941.
STRING9606.ENSP00000301067.

Chemistry

ChEMBLCHEMBL2189114.

PTM databases

PhosphoSiteO14686.

Proteomic databases

MaxQBO14686.
PaxDbO14686.
PRIDEO14686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301067; ENSP00000301067; ENSG00000167548. [O14686-1]
GeneID8085.
KEGGhsa:8085.
UCSCuc001rta.4. human. [O14686-1]

Organism-specific databases

CTD8085.
GeneCardsGC12M049413.
GeneReviewsKMT2D.
HGNCHGNC:7133. KMT2D.
HPAHPA035977.
MIM147920. phenotype.
602113. gene.
neXtProtNX_O14686.
Orphanet2322. Kabuki syndrome.
PharmGKBPA30846.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOVERGENHBG006738.
InParanoidO14686.
KOK09187.
OMAPTQHSYT.
OrthoDBEOG7N63KQ.
PhylomeDBO14686.
TreeFamTF354317.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeO14686.
CleanExHS_MLL2.
GenevestigatorO14686.

Family and domain databases

Gene3D3.30.40.10. 5 hits.
InterProIPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR009071. HMG_box_dom.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 3 hits.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00398. HMG. 1 hit.
SM00249. PHD. 7 hits.
SM00508. PostSET. 1 hit.
SM00184. RING. 6 hits.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF47095. SSF47095. 1 hit.
SSF57903. SSF57903. 5 hits.
PROSITEPS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 5 hits.
PS50016. ZF_PHD_2. 5 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMLL2. human.
GeneWikiMLL2.
GenomeRNAi8085.
NextBio30706.
PROO14686.
SOURCESearch...

Entry information

Entry nameKMT2D_HUMAN
AccessionPrimary (citable) accession number: O14686
Secondary accession number(s): O14687
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM