Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O14686

- KMT2D_HUMAN

UniProt

O14686 - KMT2D_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone-lysine N-methyltransferase 2D

Gene

KMT2D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei5451 – 54511S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi5477 – 54771ZincBy similarity
Metal bindingi5525 – 55251ZincBy similarity
Metal bindingi5527 – 55271ZincBy similarity
Metal bindingi5532 – 55321ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri226 – 27651PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 27446RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri273 – 32351PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri276 – 32146RING-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1377 – 143054PHD-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1427 – 147751PHD-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1504 – 155956PHD-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1507 – 155751RING-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri5092 – 513746RING-type 4; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
  3. transcription regulatory region DNA binding Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin silencing Source: UniProtKB
  2. histone H3-K4 methylation Source: UniProtKB
  3. oocyte growth Source: UniProtKB
  4. oogenesis Source: UniProtKB
  5. positive regulation of cell proliferation Source: UniProtKB
  6. positive regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
  7. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  8. regulation of transcription, DNA-templated Source: UniProtKB
  9. response to estrogen Source: UniProtKB
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase 2D (EC:2.1.1.43)
Short name:
Lysine N-methyltransferase 2D
Alternative name(s):
ALL1-related protein
Myeloid/lymphoid or mixed-lineage leukemia protein 2
Gene namesi
Name:KMT2D
Synonyms:ALR, MLL2, MLL4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:7133. KMT2D.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. histone methyltransferase complex Source: MGI
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5109 – 51091C → F in KABUK1. 1 Publication
VAR_063830
Natural varianti5179 – 51791R → H in KABUK1. 1 Publication
VAR_063831
Natural varianti5210 – 52101Y → C in KABUK1. 1 Publication
VAR_064378
Natural varianti5214 – 52141R → H in KABUK1. 1 Publication
VAR_063832
Natural varianti5340 – 53401R → L in KABUK1. 1 Publication
VAR_063833
Natural varianti5428 – 54281G → D in KABUK1. 1 Publication
VAR_064379
Natural varianti5464 – 54641T → M in KABUK1. 1 Publication
VAR_063834

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi147920. phenotype.
Orphaneti2322. Kabuki syndrome.
PharmGKBiPA30846.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 55375537Histone-lysine N-methyltransferase 2DPRO_0000124878Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271Phosphoserine1 Publication
Modified residuei1606 – 16061Phosphoserine1 Publication
Modified residuei1671 – 16711Phosphoserine2 Publications
Modified residuei2246 – 22461N6-acetyllysine1 Publication
Modified residuei2274 – 22741Phosphoserine3 Publications
Modified residuei2309 – 23091Phosphoserine1 Publication
Modified residuei2311 – 23111Phosphoserine1 Publication
Modified residuei3079 – 30791N6-acetyllysine1 Publication
Modified residuei3130 – 31301Phosphoserine1 Publication
Modified residuei3197 – 31971Phosphothreonine3 Publications
Modified residuei3199 – 31991Phosphoserine1 Publication
Modified residuei3433 – 34331N6-acetyllysine1 Publication
Modified residuei4215 – 42151Phosphoserine1 Publication
Modified residuei4359 – 43591Phosphoserine2 Publications
Modified residuei4465 – 44651N6-acetyllysine1 Publication
Modified residuei4738 – 47381Phosphoserine3 Publications
Modified residuei4776 – 47761N6-acetyllysine1 Publication
Modified residuei4822 – 48221Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO14686.
PaxDbiO14686.
PRIDEiO14686.

PTM databases

PhosphoSiteiO14686.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO14686.
CleanExiHS_MLL2.
ExpressionAtlasiO14686. baseline.
GenevestigatoriO14686.

Organism-specific databases

HPAiHPA035977.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033723EBI-996065,EBI-78473
NCOA6Q146866EBI-996065,EBI-78670

Protein-protein interaction databases

BioGridi113758. 26 interactions.
DIPiDIP-37875N.
IntActiO14686. 16 interactions.
MINTiMINT-1192941.
STRINGi9606.ENSP00000301067.

Structurei

Secondary structure

1
5537
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5339 – 53413Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UVKX-ray1.40B5337-5347[»]
4ERQX-ray1.91D/E/F5333-5346[»]
ProteinModelPortaliO14686.
SMRiO14686. Positions 220-323, 2000-2077.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati442 – 44651
Repeati460 – 46452
Repeati469 – 47353
Repeati496 – 50054
Repeati504 – 50855
Repeati521 – 52556
Repeati555 – 55957
Repeati564 – 56858
Repeati573 – 57759
Repeati582 – 586510
Repeati609 – 613511
Repeati618 – 622512
Repeati627 – 631513
Repeati645 – 649514
Repeati663 – 667515
Domaini5175 – 523561FYR N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini5236 – 532186FYR C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini5397 – 5513117SETPROSITE-ProRule annotationAdd
BLAST
Domaini5521 – 553717Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni439 – 66823015 X 5 AA repeats of S/P-P-P-E/P-E/AAdd
BLAST
Regioni5474 – 54752S-adenosyl-L-methionine bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2669 – 270739Sequence AnalysisAdd
BLAST
Coiled coili3249 – 328234Sequence AnalysisAdd
BLAST
Coiled coili3562 – 361453Sequence AnalysisAdd
BLAST
Coiled coili3714 – 375037Sequence AnalysisAdd
BLAST
Coiled coili3897 – 397579Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2686 – 26905LXXLL motif 1
Motifi3038 – 30425LXXLL motif 2
Motifi4222 – 423615LXXLL motif 3Add
BLAST
Motifi4253 – 42575LXXLL motif 4
Motifi4463 – 44675LXXLL motif 5
Motifi4990 – 49945LXXLL motif 6

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi229 – 32698Cys-richAdd
BLAST
Compositional biasi374 – 1197824Pro-richAdd
BLAST
Compositional biasi1290 – 132839Arg-richAdd
BLAST
Compositional biasi1351 – 13555Poly-Glu
Compositional biasi1397 – 1510114Cys-richAdd
BLAST
Compositional biasi2107 – 2626520Pro-richAdd
BLAST
Compositional biasi2385 – 23928Poly-Pro
Compositional biasi2707 – 27137Poly-Ala
Compositional biasi2811 – 282212Gln-richAdd
BLAST
Compositional biasi2862 – 2978117Pro-richAdd
BLAST
Compositional biasi3261 – 42751015Gln-richAdd
BLAST
Compositional biasi4241 – 4360120Pro-richAdd
BLAST
Compositional biasi4909 – 497769Pro-richAdd
BLAST
Compositional biasi5494 – 54974Poly-Ile

Domaini

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

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation
Contains 1 FYR C-terminal domain.PROSITE-ProRule annotation
Contains 1 FYR N-terminal domain.PROSITE-ProRule annotation
Contains 5 PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 4 RING-type zinc fingers.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri226 – 27651PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 27446RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri273 – 32351PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri276 – 32146RING-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1377 – 143054PHD-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1427 – 147751PHD-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1504 – 155956PHD-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1507 – 155751RING-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri5092 – 513746RING-type 4; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000119228.
HOVERGENiHBG006738.
InParanoidiO14686.
KOiK09187.
OMAiPTQHSYT.
OrthoDBiEOG7N63KQ.
PhylomeDBiO14686.
TreeFamiTF354317.

Family and domain databases

Gene3Di3.30.40.10. 5 hits.
InterProiIPR003889. 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]
PfamiPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 3 hits.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00542. 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]
SUPFAMiSSF47095. SSF47095. 1 hit.
SSF57903. SSF57903. 5 hits.
PROSITEiPS51543. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14686-1) [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.

« Hide

        10         20         30         40         50
MDSQKLAGED KDSEPAADGP AASEDPSATE SDLPNPHVGE VSVLSSGSPR
60 70 80 90 100
LQETPQDCSG GPVRRCALCN CGEPSLHGQR ELRRFELPFD WPRCPVVSPG
110 120 130 140 150
GSPGPNEAVL PSEDLSQIGF PEGLTPAHLG EPGGSCWAHH WCAAWSAGVW
160 170 180 190 200
GQEGPELCGV DKAIFSGISQ RCSHCTRLGA SIPCRSPGCP RLYHFPCATA
210 220 230 240 250
SGSFLSMKTL QLLCPEHSEG AAYLEEARCA VCEGPGELCD LFFCTSCGHH
260 270 280 290 300
YHGACLDTAL TARKRAGWQC PECKVCQACR KPGNDSKMLV CETCDKGYHT
310 320 330 340 350
FCLKPPMEEL PAHSWKCKAC RVCRACGAGS AELNPNSEWF ENYSLCHRCH
360 370 380 390 400
KAQGGQTIRS VAEQHTPVCS RFSPPEPGDT PTDEPDALYV ACQGQPKGGH
410 420 430 440 450
VTSMQPKEPG PLQCEAKPLG KAGVQLEPQL EAPLNEEMPL LPPPEESPLS
460 470 480 490 500
PPPEESPTSP PPEASRLSPP PEELPASPLP EALHLSRPLE ESPLSPPPEE
510 520 530 540 550
SPLSPPPESS PFSPLEESPL SPPEESPPSP ALETPLSPPP EASPLSPPFE
560 570 580 590 600
ESPLSPPPEE LPTSPPPEAS RLSPPPEESP MSPPPEESPM SPPPEASRLF
610 620 630 640 650
PPFEESPLSP PPEESPLSPP PEASRLSPPP EDSPMSPPPE ESPMSPPPEV
660 670 680 690 700
SRLSPLPVVS RLSPPPEESP LSPPPEESPT SPPPEASRLS PPPEDSPTSP
710 720 730 740 750
PPEDSPASPP PEDSLMSLPL EESPLLPLPE EPQLCPRSEG PHLSPRPEEP
760 770 780 790 800
HLSPRPEEPH LSPQAEEPHL SPQPEEPCLC AVPEEPHLSP QAEGPHLSPQ
810 820 830 840 850
PEELHLSPQT EEPHLSPVPE EPCLSPQPEE SHLSPQSEEP CLSPRPEESH
860 870 880 890 900
LSPELEKPPL SPRPEKPPEE PGQCPAPEEL PLFPPPGEPS LSPLLGEPAL
910 920 930 940 950
SEPGEPPLSP LPEELPLSPS GEPSLSPQLM PPDPLPPPLS PIITAAAPPA
960 970 980 990 1000
LSPLGELEYP FGAKGDSDPE SPLAAPILET PISPPPEANC TDPEPVPPMI
1010 1020 1030 1040 1050
LPPSPGSPVG PASPILMEPL PPQCSPLLQH SLVPQNSPPS QCSPPALPLS
1060 1070 1080 1090 1100
VPSPLSPIGK VVGVSDEAEL HEMETEKVSE PECPALEPSA TSPLPSPMGD
1110 1120 1130 1140 1150
LSCPAPSPAP ALDDFSGLGE DTAPLDGIDA PGSQPEPGQT PGSLASELKG
1160 1170 1180 1190 1200
SPVLLDPEEL APVTPMEVYP ECKQTAGQGS PCEEQEEPRA PVAPTPPTLI
1210 1220 1230 1240 1250
KSDIVNEISN LSQGDASASF PGSEPLLGSP DPEGGGSLSM ELGVSTDVSP
1260 1270 1280 1290 1300
ARDEGSLRLC TDSLPETDDS LLCDAGTAIS GGKAEGEKGR RRSSPARSRI
1310 1320 1330 1340 1350
KQGRSSSFPG RRRPRGGAHG GRGRGRARLK STASSIETLV VADIDSSPSK
1360 1370 1380 1390 1400
EEEEEDDDTM QNTVVLFSNT DKFVLMQDMC VVCGSFGRGA EGHLLACSQC
1410 1420 1430 1440 1450
SQCYHPYCVN SKITKVMLLK GWRCVECIVC EVCGQASDPS RLLLCDDCDI
1460 1470 1480 1490 1500
SYHTYCLDPP LLTVPKGGWK CKWCVSCMQC GAASPGFHCE WQNSYTHCGP
1510 1520 1530 1540 1550
CASLVTCPIC HAPYVEEDLL IQCRHCERWM HAGCESLFTE DDVEQAADEG
1560 1570 1580 1590 1600
FDCVSCQPYV VKPVAPVAPP ELVPMKVKEP EPQYFRFEGV WLTETGMALL
1610 1620 1630 1640 1650
RNLTMSPLHK RRQRRGRLGL PGEAGLEGSE PSDALGPDDK KDGDLDTDEL
1660 1670 1680 1690 1700
LKGEGGVEHM ECEIKLEGPV SPDVEPGKEE TEESKKRKRK PYRPGIGGFM
1710 1720 1730 1740 1750
VRQRKSHTRT KKGPAAQAEV LSGDGQPDEV IPADLPAEGA VEQSLAEGDE
1760 1770 1780 1790 1800
KKKQQRRGRK KSKLEDMFPA YLQEAFFGKE LLDLSRKALF AVGVGRPSFG
1810 1820 1830 1840 1850
LGTPKAKGDG GSERKELPTS QKGDDGPDIA DEESRGLEGK ADTPGPEDGG
1860 1870 1880 1890 1900
VKASPVPSDP EKPGTPGEGM LSSDLDRIST EELPKMESKD LQQLFKDVLG
1910 1920 1930 1940 1950
SEREQHLGCG TPGLEGSRTP LQRPFLQGGL PLGNLPSSSP MDSYPGLCQS
1960 1970 1980 1990 2000
PFLDSRERGG FFSPEPGEPD SPWTGSGGTT PSTPTTPTTE GEGDGLSYNQ
2010 2020 2030 2040 2050
RSLQRWEKDE ELGQLSTISP VLYANINFPN LKQDYPDWSS RCKQIMKLWR
2060 2070 2080 2090 2100
KVPAADKAPY LQKAKDNRAA HRINKVQKQA ESQINKQTKV GDIARKTDRP
2110 2120 2130 2140 2150
ALHLRIPPQP GALGSPPPAA APTIFIGSPT TPAGLSTSAD GFLKPPAGSV
2160 2170 2180 2190 2200
PGPDSPGELF LKLPPQVPAQ VPSQDPFGLA PAYPLEPRFP TAPPTYPPYP
2210 2220 2230 2240 2250
SPTGAPAQPP MLGASSRPGA GQPGEFHTTP PGTPRHQPST PDPFLKPRCP
2260 2270 2280 2290 2300
SLDNLAVPES PGVGGGKASE PLLSPPPFGE SRKALEVKKE ELGASSPSYG
2310 2320 2330 2340 2350
PPNLGFVDSP SSGTHLGGLE LKTPDVFKAP LTPRASQVEP QSPGLGLRPQ
2360 2370 2380 2390 2400
EPPPAQALAP SPPSHPDIFR PGSYTDPYAQ PPLTPRPQPP PPESCCALPP
2410 2420 2430 2440 2450
RSLPSDPFSR VPASPQSQSS SQSPLTPRPL SAEAFCPSPV TPRFQSPDPY
2460 2470 2480 2490 2500
SRPPSRPQSR DPFAPLHKPP RPQPPEVAFK AGSLAHTSLG AGGFPAALPA
2510 2520 2530 2540 2550
GPAGELHAKV PSGQPPNFVR SPGTGAFVGT PSPMRFTFPQ AVGEPSLKPP
2560 2570 2580 2590 2600
VPQPGLPPPH GINSHFGPGP TLGKPQSTNY TVATGNFHPS GSPLGPSSGS
2610 2620 2630 2640 2650
TGESYGLSPL RPPSVLPPPA PDGSLPYLSH GASQRSGITS PVEKREDPGT
2660 2670 2680 2690 2700
GMGSSLATAE LPGTQDPGMS GLSQTELEKQ RQRQRLRELL IRQQIQRNTL
2710 2720 2730 2740 2750
RQEKETAAAA AGAVGPPGSW GAEPSSPAFE QLSRGQTPFA GTQDKSSLVG
2760 2770 2780 2790 2800
LPPSKLSGPI LGPGSFPSDD RLSRPPPPAT PSSMDVNSRQ LVGGSQAFYQ
2810 2820 2830 2840 2850
RAPYPGSLPL QQQQQQLWQQ QQATAATSMR FAMSARFPST PGPELGRQAL
2860 2870 2880 2890 2900
GSPLAGISTR LPGPGEPVPG PAGPAQFIEL RHNVQKGLGP GGTPFPGQGP
2910 2920 2930 2940 2950
PQRPRFYPVS EDPHRLAPEG LRGLAVSGLP PQKPSAPPAP ELNNSLHPTP
2960 2970 2980 2990 3000
HTKGPTLPTG LELVNRPPSS TELGRPNPLA LEAGKLPCED PELDDDFDAH
3010 3020 3030 3040 3050
KALEDDEELA HLGLGVDVAK GDDELGTLEN LETNDPHLDD LLNGDEFDLL
3060 3070 3080 3090 3100
AYTDPELDTG DKKDIFNEHL RLVESANEKA EREALLRGVE PGPLGPEERP
3110 3120 3130 3140 3150
PPAADASEPR LASVLPEVKP KVEEGGRHPS PCQFTIATPK VEPAPAANSL
3160 3170 3180 3190 3200
GLGLKPGQSM MGSRDTRMGT GPFSSSGHTA EKASFGATGG PPAHLLTPSP
3210 3220 3230 3240 3250
LSGPGGSSLL EKFELESGAL TLPGGPAASG DELDKMESSL VASELPLLIE
3260 3270 3280 3290 3300
DLLEHEKKEL QKKQQLSAQL QPAQQQQQQQ QQHSLLSAPG PAQAMSLPHE
3310 3320 3330 3340 3350
GSSPSLAGSQ QQLSLGLAGA RQPGLPQPLM PTQPPAHALQ QRLAPSMAMV
3360 3370 3380 3390 3400
SNQGHMLSGQ HGGQAGLVPQ QSSQPVLSQK PMGTMPPSMC MKPQQLAMQQ
3410 3420 3430 3440 3450
QLANSFFPDT DLDKFAAEDI IDPIAKAKMV ALKGIKKVMA QGSIGVAPGM
3460 3470 3480 3490 3500
NRQQVSLLAQ RLSGGPSSDL QNHVAAGSGQ ERSAGDPSQP RPNPPTFAQG
3510 3520 3530 3540 3550
VINEADQRQY EEWLFHTQQL LQMQLKVLEE QIGVHRKSRK ALCAKQRTAK
3560 3570 3580 3590 3600
KAGREFPEAD AEKLKLVTEQ QSKIQKQLDQ VRKQQKEHTN LMAEYRNKQQ
3610 3620 3630 3640 3650
QQQQQQQQQQ QQHSAVLALS PSQSPRLLTK LPGQLLPGHG LQPPQGPPGG
3660 3670 3680 3690 3700
QAGGLRLTPG GMALPGQPGG PFLNTALAQQ QQQQHSGGAG SLAGPSGGFF
3710 3720 3730 3740 3750
PGNLALRSLG PDSRLLQERQ LQLQQQRMQL AQKLQQQQQQ QQQQQHLLGQ
3760 3770 3780 3790 3800
VAIQQQQQQG PGVQTNQALG PKPQGLMPPS SHQGLLVQQL SPQPPQGPQG
3810 3820 3830 3840 3850
MLGPAQVAVL QQQHPGALGP QGPHRQVLMT QSRVLSSPQL AQQGQGLMGH
3860 3870 3880 3890 3900
RLVTAQQQQQ QQQHQQQGSM AGLSHLQQSL MSHSGQPKLS AQPMGSLQQL
3910 3920 3930 3940 3950
QQQQQLQQQQ QLQQQQQQQL QQQQQLQQQQ LQQQQQQQQL QQQQQQQLQQ
3960 3970 3980 3990 4000
QQQQLQQQQQ QQQQQFQQQQ QQQQMGLLNQ SRTLLSPQQQ QQQQVALGPG
4010 4020 4030 4040 4050
MPAKPLQHFS SPGALGPTLL LTGKEQNTVD PAVSSEATEG PSTHQGGPLA
4060 4070 4080 4090 4100
IGTTPESMAT EPGEVKPSLS GDSQLLLVQP QPQPQPSSLQ LQPPLRLPGQ
4110 4120 4130 4140 4150
QQQQVSLLHT AGGGSHGQLG SGSSSEASSV PHLLAQPSVS LGDQPGSMTQ
4160 4170 4180 4190 4200
NLLGPQQPML ERPMQNNTGP QPPKPGPVLQ SGQGLPGVGI MPTVGQLRAQ
4210 4220 4230 4240 4250
LQGVLAKNPQ LRHLSPQQQQ QLQALLMQRQ LQQSQAVRQT PPYQEPGTQT
4260 4270 4280 4290 4300
SPLQGLLGCQ PQLGGFPGPQ TGPLQELGAG PRPQGPPRLP APPGALSTGP
4310 4320 4330 4340 4350
VLGPVHPTPP PSSPQEPKRP SQLPSPSSQL PTEAQLPPTH PGTPKPQGPT
4360 4370 4380 4390 4400
LEPPPGRVSP AAAQLADTLF SKGLGPWDPP DNLAETQKPE QSSLVPGHLD
4410 4420 4430 4440 4450
QVNGQVVPEA SQLSIKQEPR EEPCALGAQS VKREANGEPI GAPGTSNHLL
4460 4470 4480 4490 4500
LAGPRSEAGH LLLQKLLRAK NVQLSTGRGS EGLRAEINGH IDSKLAGLEQ
4510 4520 4530 4540 4550
KLQGTPSNKE DAAARKPLTP KPKRVQKASD RLVSSRKKLR KEDGVRASEA
4560 4570 4580 4590 4600
LLKQLKQELS LLPLTEPAIT ANFSLFAPFG SGCPVNGQSQ LRGAFGSGAL
4610 4620 4630 4640 4650
PTGPDYYSQL LTKNNLSNPP TPPSSLPPTP PPSVQQKMVN GVTPSEELGE
4660 4670 4680 4690 4700
HPKDAASARD SERALRDTSE VKSLDLLAAL PTPPHNQTED VRMESDEDSD
4710 4720 4730 4740 4750
SPDSIVPASS PESILGEEAP RFPHLGSGRW EQEDRALSPV IPLIPRASIP
4760 4770 4780 4790 4800
VFPDTKPYGA LGLEVPGKLP VTTWEKGKGS EVSVMLTVSA AAAKNLNGVM
4810 4820 4830 4840 4850
VAVAELLSMK IPNSYEVLFP ESPARAGTEP KKGEAEGPGG KEKGLEGKSP
4860 4870 4880 4890 4900
DTGPDWLKQF DAVLPGYTLK SQLDILSLLK QESPAPEPPT QHSYTYNVSN
4910 4920 4930 4940 4950
LDVRQLSAPP PEEPSPPPSP LAPSPASPPT EPLVELPTEP LAEPPVPSPL
4960 4970 4980 4990 5000
PLASSPESAR PKPRARPPEE GEDSRPPRLK KWKGVRWKRL RLLLTIQKGS
5010 5020 5030 5040 5050
GRQEDEREVA EFMEQLGTAL RPDKVPRDMR RCCFCHEEGD GATDGPARLL
5060 5070 5080 5090 5100
NLDLDLWVHL NCALWSTEVY ETQGGALMNV EVALHRGLLT KCSLCQRTGA
5110 5120 5130 5140 5150
TSSCNRMRCP NVYHFACAIR AKCMFFKDKT MLCPMHKIKG PCEQELSSFA
5160 5170 5180 5190 5200
VFRRVYIERD EVKQIASIIQ RGERLHMFRV GGLVFHAIGQ LLPHQMADFH
5210 5220 5230 5240 5250
SATALYPVGY EATRIYWSLR TNNRRCCYRC SIGENNGRPE FVIKVIEQGL
5260 5270 5280 5290 5300
EDLVFTDASP QAVWNRIIEP VAAMRKEADM LRLFPEYLKG EELFGLTVHA
5310 5320 5330 5340 5350
VLRIAESLPG VESCQNYLFR YGRHPLMELP LMINPTGCAR SEPKILTHYK
5360 5370 5380 5390 5400
RPHTLNSTSM SKAYQSTFTG ETNTPYSKQF VHSKSSQYRR LRTEWKNNVY
5410 5420 5430 5440 5450
LARSRIQGLG LYAAKDLEKH TMVIEYIGTI IRNEVANRRE KIYEEQNRGI
5460 5470 5480 5490 5500
YMFRINNEHV IDATLTGGPA RYINHSCAPN CVAEVVTFDK EDKIIIISSR
5510 5520 5530
RIPKGEELTY DYQFDFEDDQ HKIPCHCGAW NCRKWMN
Length:5,537
Mass (Da):593,389
Last modified:November 30, 2010 - v2
Checksum:i31C6DAB0A754F72A
GO
Isoform 3 (identifier: O14686-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:5,540
Mass (Da):593,677
Checksum:iBB9AC95AA8BC0DD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51K → N in AAC51734. (PubMed:9247308)Curated
Sequence conflicti14 – 141E → Q in AAC51734. (PubMed:9247308)Curated
Sequence conflicti75 – 751S → A in AAC51734. (PubMed:9247308)Curated
Sequence conflicti156 – 1561E → Q in AAC51734. (PubMed:9247308)Curated
Sequence conflicti674 – 948275Missing in AAC51734. (PubMed:9247308)CuratedAdd
BLAST
Sequence conflicti1178 – 11781Q → R in AAC51734. (PubMed:9247308)Curated
Sequence conflicti1178 – 11781Q → R in AAC51735. (PubMed:9247308)Curated
Sequence conflicti1544 – 15474EQAA → DHAP in AAC51734. (PubMed:9247308)Curated
Sequence conflicti1544 – 15474EQAA → DHAP in AAC51735. (PubMed:9247308)Curated
Sequence conflicti1761 – 17611K → R in AAC51734. (PubMed:9247308)Curated
Sequence conflicti1761 – 17611K → R in AAC51735. (PubMed:9247308)Curated
Sequence conflicti1766 – 17661D → G in AAC51734. (PubMed:9247308)Curated
Sequence conflicti1766 – 17661D → G in AAC51735. (PubMed:9247308)Curated
Sequence conflicti2171 – 21711V → A in AAC51734. (PubMed:9247308)Curated
Sequence conflicti2171 – 21711V → A in AAC51735. (PubMed:9247308)Curated
Sequence conflicti2413 – 24131A → V in AAC51734. (PubMed:9247308)Curated
Sequence conflicti2413 – 24131A → V in AAC51735. (PubMed:9247308)Curated
Sequence conflicti3079 – 30791K → E in AAC51734. (PubMed:9247308)Curated
Sequence conflicti3079 – 30791K → E in AAC51735. (PubMed:9247308)Curated
Sequence conflicti3287 – 32871S → P in AAC51734. (PubMed:9247308)Curated
Sequence conflicti3287 – 32871S → P in AAC51735. (PubMed:9247308)Curated
Sequence conflicti3319 – 33191G → V in AAC51734. (PubMed:9247308)Curated
Sequence conflicti3319 – 33191G → V in AAC51735. (PubMed:9247308)Curated
Sequence conflicti3422 – 34221D → G in AAC51734. (PubMed:9247308)Curated
Sequence conflicti3422 – 34221D → G in AAC51735. (PubMed:9247308)Curated
Sequence conflicti4478 – 44781R → Q in AAC51734. (PubMed:9247308)Curated
Sequence conflicti4478 – 44781R → Q in AAC51735. (PubMed:9247308)Curated
Sequence conflicti4747 – 47471A → D in AAC51734. (PubMed:9247308)Curated
Sequence conflicti4747 – 47471A → D in AAC51735. (PubMed:9247308)Curated
Sequence conflicti4793 – 47931A → D in AAC51734. (PubMed:9247308)Curated
Sequence conflicti4793 – 47931A → D in AAC51735. (PubMed:9247308)Curated
Sequence conflicti4826 – 48261A → G in AAC51734. (PubMed:9247308)Curated
Sequence conflicti4826 – 48261A → G in AAC51735. (PubMed:9247308)Curated
Sequence conflicti4865 – 48651P → A in AAC51734. (PubMed:9247308)Curated
Sequence conflicti4865 – 48651P → A in AAC51735. (PubMed:9247308)Curated
Sequence conflicti4871 – 48711S → R in AAC51734. (PubMed:9247308)Curated
Sequence conflicti4871 – 48711S → R in AAC51735. (PubMed:9247308)Curated
Sequence conflicti4893 – 48931S → R in AAC51734. (PubMed:9247308)Curated
Sequence conflicti4893 – 48931S → R in AAC51735. (PubMed:9247308)Curated
Sequence conflicti4974 – 49741S → T in AAC51734. (PubMed:9247308)Curated
Sequence conflicti4974 – 49741S → T in AAC51735. (PubMed:9247308)Curated
Sequence conflicti5116 – 51161A → G in AAC51734. (PubMed:9247308)Curated
Sequence conflicti5116 – 51161A → G in AAC51735. (PubMed:9247308)Curated
Sequence conflicti5522 – 55221K → E in AAC51734. (PubMed:9247308)Curated
Sequence conflicti5522 – 55221K → E in AAC51735. (PubMed:9247308)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti476 – 4761A → T.
Corresponds to variant rs1064210 [ dbSNP | Ensembl ].
VAR_057359
Natural varianti692 – 6921P → T.1 Publication
Corresponds to variant rs202076833 [ dbSNP | Ensembl ].
VAR_064370
Natural varianti813 – 8131P → L.1 Publication
Corresponds to variant rs75226229 [ dbSNP | Ensembl ].
VAR_064371
Natural varianti2382 – 23821P → S.1 Publication
Corresponds to variant rs3741626 [ dbSNP | Ensembl ].
VAR_064372
Natural varianti2460 – 24601R → C.1 Publication
VAR_064373
Natural varianti2557 – 25571P → L.1 Publication
Corresponds to variant rs189888707 [ dbSNP | Ensembl ].
VAR_064374
Natural varianti3398 – 33981M → V.1 Publication
Corresponds to variant rs75937132 [ dbSNP | Ensembl ].
VAR_064375
Natural varianti3419 – 34191D → G.1 Publication
Corresponds to variant rs146044282 [ dbSNP | Ensembl ].
VAR_064376
Natural varianti4357 – 43571R → S.1 Publication
VAR_064377
Natural varianti5109 – 51091C → F in KABUK1. 1 Publication
VAR_063830
Natural varianti5179 – 51791R → H in KABUK1. 1 Publication
VAR_063831
Natural varianti5210 – 52101Y → C in KABUK1. 1 Publication
VAR_064378
Natural varianti5214 – 52141R → H in KABUK1. 1 Publication
VAR_063832
Natural varianti5224 – 52241R → H.
Corresponds to variant rs3782356 [ dbSNP | Ensembl ].
VAR_017115
Natural varianti5340 – 53401R → L in KABUK1. 1 Publication
VAR_063833
Natural varianti5428 – 54281G → D in KABUK1. 1 Publication
VAR_064379
Natural varianti5464 – 54641T → M in KABUK1. 1 Publication
VAR_063834

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1729 – 17291E → EGET in isoform 3. 1 PublicationVSP_008560

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF010403 mRNA. Translation: AAC51734.1.
AF010404 mRNA. Translation: AAC51735.1.
AC011603 Genomic DNA. No translation available.
CCDSiCCDS44873.1. [O14686-1]
PIRiT03454.
T03455.
RefSeqiNP_003473.3. NM_003482.3. [O14686-1]
XP_005269219.1. XM_005269162.2. [O14686-1]
XP_006719677.1. XM_006719614.1. [O14686-3]
UniGeneiHs.731384.

Genome annotation databases

EnsembliENST00000301067; ENSP00000301067; ENSG00000167548. [O14686-1]
GeneIDi8085.
KEGGihsa:8085.
UCSCiuc001rta.4. human. [O14686-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF010403 mRNA. Translation: AAC51734.1 .
AF010404 mRNA. Translation: AAC51735.1 .
AC011603 Genomic DNA. No translation available.
CCDSi CCDS44873.1. [O14686-1 ]
PIRi T03454.
T03455.
RefSeqi NP_003473.3. NM_003482.3. [O14686-1 ]
XP_005269219.1. XM_005269162.2. [O14686-1 ]
XP_006719677.1. XM_006719614.1. [O14686-3 ]
UniGenei Hs.731384.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UVK X-ray 1.40 B 5337-5347 [» ]
4ERQ X-ray 1.91 D/E/F 5333-5346 [» ]
ProteinModelPortali O14686.
SMRi O14686. Positions 220-323, 2000-2077.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113758. 26 interactions.
DIPi DIP-37875N.
IntActi O14686. 16 interactions.
MINTi MINT-1192941.
STRINGi 9606.ENSP00000301067.

Chemistry

ChEMBLi CHEMBL2189114.

PTM databases

PhosphoSitei O14686.

Proteomic databases

MaxQBi O14686.
PaxDbi O14686.
PRIDEi O14686.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301067 ; ENSP00000301067 ; ENSG00000167548 . [O14686-1 ]
GeneIDi 8085.
KEGGi hsa:8085.
UCSCi uc001rta.4. human. [O14686-1 ]

Organism-specific databases

CTDi 8085.
GeneCardsi GC12M049413.
GeneReviewsi KMT2D.
HGNCi HGNC:7133. KMT2D.
HPAi HPA035977.
MIMi 147920. phenotype.
602113. gene.
neXtProti NX_O14686.
Orphaneti 2322. Kabuki syndrome.
PharmGKBi PA30846.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00760000119228.
HOVERGENi HBG006738.
InParanoidi O14686.
KOi K09187.
OMAi PTQHSYT.
OrthoDBi EOG7N63KQ.
PhylomeDBi O14686.
TreeFami TF354317.

Enzyme and pathway databases

Reactomei REACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.

Miscellaneous databases

ChiTaRSi MLL2. human.
GeneWikii MLL2.
GenomeRNAii 8085.
NextBioi 30706.
PROi O14686.
SOURCEi Search...

Gene expression databases

Bgeei O14686.
CleanExi HS_MLL2.
ExpressionAtlasi O14686. baseline.
Genevestigatori O14686.

Family and domain databases

Gene3Di 3.30.40.10. 5 hits.
InterProi IPR003889. 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 ]
Pfami PF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 3 hits.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00542. 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 ]
SUPFAMi SSF47095. SSF47095. 1 hit.
SSF57903. SSF57903. 5 hits.
PROSITEi PS51543. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: FUNCTION, IDENTIFICATION IN THE MLL2/3 COMPLEX.
  9. 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. 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. 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. Cited for: VARIANTS KABUK1 PHE-5109; HIS-5179; HIS-5214; LEU-5340 AND MET-5464.

Entry informationi

Entry nameiKMT2D_HUMAN
AccessioniPrimary (citable) accession number: O14686
Secondary accession number(s): O14687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: November 30, 2010
Last modified: October 29, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

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.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3