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O14686

- KMT2D_HUMAN

UniProt

O14686 - KMT2D_HUMAN

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Protein

Histone-lysine N-methyltransferase 2D

Gene
KMT2D, ALR, MLL2, MLL4
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-methionine By similarity
Metal bindingi5477 – 54771Zinc By similarity
Metal bindingi5525 – 55251Zinc By similarity
Metal bindingi5527 – 55271Zinc By similarity
Metal bindingi5532 – 55321Zinc By similarity

Regions

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

GO - Molecular functioni

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

GO - Biological processi

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
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. 25 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 – 53413

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.

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-terminalAdd
BLAST
Domaini5236 – 532186FYR C-terminalAdd
BLAST
Domaini5397 – 5513117SETAdd
BLAST
Domaini5521 – 553717Post-SETAdd
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 binding By similarity

Coiled coil

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

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

Zinc finger

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

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG2940.
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.

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MDSQKLAGED KDSEPAADGP AASEDPSATE SDLPNPHVGE VSVLSSGSPR     50
LQETPQDCSG GPVRRCALCN CGEPSLHGQR ELRRFELPFD WPRCPVVSPG 100
GSPGPNEAVL PSEDLSQIGF PEGLTPAHLG EPGGSCWAHH WCAAWSAGVW 150
GQEGPELCGV DKAIFSGISQ RCSHCTRLGA SIPCRSPGCP RLYHFPCATA 200
SGSFLSMKTL QLLCPEHSEG AAYLEEARCA VCEGPGELCD LFFCTSCGHH 250
YHGACLDTAL TARKRAGWQC PECKVCQACR KPGNDSKMLV CETCDKGYHT 300
FCLKPPMEEL PAHSWKCKAC RVCRACGAGS AELNPNSEWF ENYSLCHRCH 350
KAQGGQTIRS VAEQHTPVCS RFSPPEPGDT PTDEPDALYV ACQGQPKGGH 400
VTSMQPKEPG PLQCEAKPLG KAGVQLEPQL EAPLNEEMPL LPPPEESPLS 450
PPPEESPTSP PPEASRLSPP PEELPASPLP EALHLSRPLE ESPLSPPPEE 500
SPLSPPPESS PFSPLEESPL SPPEESPPSP ALETPLSPPP EASPLSPPFE 550
ESPLSPPPEE LPTSPPPEAS RLSPPPEESP MSPPPEESPM SPPPEASRLF 600
PPFEESPLSP PPEESPLSPP PEASRLSPPP EDSPMSPPPE ESPMSPPPEV 650
SRLSPLPVVS RLSPPPEESP LSPPPEESPT SPPPEASRLS PPPEDSPTSP 700
PPEDSPASPP PEDSLMSLPL EESPLLPLPE EPQLCPRSEG PHLSPRPEEP 750
HLSPRPEEPH LSPQAEEPHL SPQPEEPCLC AVPEEPHLSP QAEGPHLSPQ 800
PEELHLSPQT EEPHLSPVPE EPCLSPQPEE SHLSPQSEEP CLSPRPEESH 850
LSPELEKPPL SPRPEKPPEE PGQCPAPEEL PLFPPPGEPS LSPLLGEPAL 900
SEPGEPPLSP LPEELPLSPS GEPSLSPQLM PPDPLPPPLS PIITAAAPPA 950
LSPLGELEYP FGAKGDSDPE SPLAAPILET PISPPPEANC TDPEPVPPMI 1000
LPPSPGSPVG PASPILMEPL PPQCSPLLQH SLVPQNSPPS QCSPPALPLS 1050
VPSPLSPIGK VVGVSDEAEL HEMETEKVSE PECPALEPSA TSPLPSPMGD 1100
LSCPAPSPAP ALDDFSGLGE DTAPLDGIDA PGSQPEPGQT PGSLASELKG 1150
SPVLLDPEEL APVTPMEVYP ECKQTAGQGS PCEEQEEPRA PVAPTPPTLI 1200
KSDIVNEISN LSQGDASASF PGSEPLLGSP DPEGGGSLSM ELGVSTDVSP 1250
ARDEGSLRLC TDSLPETDDS LLCDAGTAIS GGKAEGEKGR RRSSPARSRI 1300
KQGRSSSFPG RRRPRGGAHG GRGRGRARLK STASSIETLV VADIDSSPSK 1350
EEEEEDDDTM QNTVVLFSNT DKFVLMQDMC VVCGSFGRGA EGHLLACSQC 1400
SQCYHPYCVN SKITKVMLLK GWRCVECIVC EVCGQASDPS RLLLCDDCDI 1450
SYHTYCLDPP LLTVPKGGWK CKWCVSCMQC GAASPGFHCE WQNSYTHCGP 1500
CASLVTCPIC HAPYVEEDLL IQCRHCERWM HAGCESLFTE DDVEQAADEG 1550
FDCVSCQPYV VKPVAPVAPP ELVPMKVKEP EPQYFRFEGV WLTETGMALL 1600
RNLTMSPLHK RRQRRGRLGL PGEAGLEGSE PSDALGPDDK KDGDLDTDEL 1650
LKGEGGVEHM ECEIKLEGPV SPDVEPGKEE TEESKKRKRK PYRPGIGGFM 1700
VRQRKSHTRT KKGPAAQAEV LSGDGQPDEV IPADLPAEGA VEQSLAEGDE 1750
KKKQQRRGRK KSKLEDMFPA YLQEAFFGKE LLDLSRKALF AVGVGRPSFG 1800
LGTPKAKGDG GSERKELPTS QKGDDGPDIA DEESRGLEGK ADTPGPEDGG 1850
VKASPVPSDP EKPGTPGEGM LSSDLDRIST EELPKMESKD LQQLFKDVLG 1900
SEREQHLGCG TPGLEGSRTP LQRPFLQGGL PLGNLPSSSP MDSYPGLCQS 1950
PFLDSRERGG FFSPEPGEPD SPWTGSGGTT PSTPTTPTTE GEGDGLSYNQ 2000
RSLQRWEKDE ELGQLSTISP VLYANINFPN LKQDYPDWSS RCKQIMKLWR 2050
KVPAADKAPY LQKAKDNRAA HRINKVQKQA ESQINKQTKV GDIARKTDRP 2100
ALHLRIPPQP GALGSPPPAA APTIFIGSPT TPAGLSTSAD GFLKPPAGSV 2150
PGPDSPGELF LKLPPQVPAQ VPSQDPFGLA PAYPLEPRFP TAPPTYPPYP 2200
SPTGAPAQPP MLGASSRPGA GQPGEFHTTP PGTPRHQPST PDPFLKPRCP 2250
SLDNLAVPES PGVGGGKASE PLLSPPPFGE SRKALEVKKE ELGASSPSYG 2300
PPNLGFVDSP SSGTHLGGLE LKTPDVFKAP LTPRASQVEP QSPGLGLRPQ 2350
EPPPAQALAP SPPSHPDIFR PGSYTDPYAQ PPLTPRPQPP PPESCCALPP 2400
RSLPSDPFSR VPASPQSQSS SQSPLTPRPL SAEAFCPSPV TPRFQSPDPY 2450
SRPPSRPQSR DPFAPLHKPP RPQPPEVAFK AGSLAHTSLG AGGFPAALPA 2500
GPAGELHAKV PSGQPPNFVR SPGTGAFVGT PSPMRFTFPQ AVGEPSLKPP 2550
VPQPGLPPPH GINSHFGPGP TLGKPQSTNY TVATGNFHPS GSPLGPSSGS 2600
TGESYGLSPL RPPSVLPPPA PDGSLPYLSH GASQRSGITS PVEKREDPGT 2650
GMGSSLATAE LPGTQDPGMS GLSQTELEKQ RQRQRLRELL IRQQIQRNTL 2700
RQEKETAAAA AGAVGPPGSW GAEPSSPAFE QLSRGQTPFA GTQDKSSLVG 2750
LPPSKLSGPI LGPGSFPSDD RLSRPPPPAT PSSMDVNSRQ LVGGSQAFYQ 2800
RAPYPGSLPL QQQQQQLWQQ QQATAATSMR FAMSARFPST PGPELGRQAL 2850
GSPLAGISTR LPGPGEPVPG PAGPAQFIEL RHNVQKGLGP GGTPFPGQGP 2900
PQRPRFYPVS EDPHRLAPEG LRGLAVSGLP PQKPSAPPAP ELNNSLHPTP 2950
HTKGPTLPTG LELVNRPPSS TELGRPNPLA LEAGKLPCED PELDDDFDAH 3000
KALEDDEELA HLGLGVDVAK GDDELGTLEN LETNDPHLDD LLNGDEFDLL 3050
AYTDPELDTG DKKDIFNEHL RLVESANEKA EREALLRGVE PGPLGPEERP 3100
PPAADASEPR LASVLPEVKP KVEEGGRHPS PCQFTIATPK VEPAPAANSL 3150
GLGLKPGQSM MGSRDTRMGT GPFSSSGHTA EKASFGATGG PPAHLLTPSP 3200
LSGPGGSSLL EKFELESGAL TLPGGPAASG DELDKMESSL VASELPLLIE 3250
DLLEHEKKEL QKKQQLSAQL QPAQQQQQQQ QQHSLLSAPG PAQAMSLPHE 3300
GSSPSLAGSQ QQLSLGLAGA RQPGLPQPLM PTQPPAHALQ QRLAPSMAMV 3350
SNQGHMLSGQ HGGQAGLVPQ QSSQPVLSQK PMGTMPPSMC MKPQQLAMQQ 3400
QLANSFFPDT DLDKFAAEDI IDPIAKAKMV ALKGIKKVMA QGSIGVAPGM 3450
NRQQVSLLAQ RLSGGPSSDL QNHVAAGSGQ ERSAGDPSQP RPNPPTFAQG 3500
VINEADQRQY EEWLFHTQQL LQMQLKVLEE QIGVHRKSRK ALCAKQRTAK 3550
KAGREFPEAD AEKLKLVTEQ QSKIQKQLDQ VRKQQKEHTN LMAEYRNKQQ 3600
QQQQQQQQQQ QQHSAVLALS PSQSPRLLTK LPGQLLPGHG LQPPQGPPGG 3650
QAGGLRLTPG GMALPGQPGG PFLNTALAQQ QQQQHSGGAG SLAGPSGGFF 3700
PGNLALRSLG PDSRLLQERQ LQLQQQRMQL AQKLQQQQQQ QQQQQHLLGQ 3750
VAIQQQQQQG PGVQTNQALG PKPQGLMPPS SHQGLLVQQL SPQPPQGPQG 3800
MLGPAQVAVL QQQHPGALGP QGPHRQVLMT QSRVLSSPQL AQQGQGLMGH 3850
RLVTAQQQQQ QQQHQQQGSM AGLSHLQQSL MSHSGQPKLS AQPMGSLQQL 3900
QQQQQLQQQQ QLQQQQQQQL QQQQQLQQQQ LQQQQQQQQL QQQQQQQLQQ 3950
QQQQLQQQQQ QQQQQFQQQQ QQQQMGLLNQ SRTLLSPQQQ QQQQVALGPG 4000
MPAKPLQHFS SPGALGPTLL LTGKEQNTVD PAVSSEATEG PSTHQGGPLA 4050
IGTTPESMAT EPGEVKPSLS GDSQLLLVQP QPQPQPSSLQ LQPPLRLPGQ 4100
QQQQVSLLHT AGGGSHGQLG SGSSSEASSV PHLLAQPSVS LGDQPGSMTQ 4150
NLLGPQQPML ERPMQNNTGP QPPKPGPVLQ SGQGLPGVGI MPTVGQLRAQ 4200
LQGVLAKNPQ LRHLSPQQQQ QLQALLMQRQ LQQSQAVRQT PPYQEPGTQT 4250
SPLQGLLGCQ PQLGGFPGPQ TGPLQELGAG PRPQGPPRLP APPGALSTGP 4300
VLGPVHPTPP PSSPQEPKRP SQLPSPSSQL PTEAQLPPTH PGTPKPQGPT 4350
LEPPPGRVSP AAAQLADTLF SKGLGPWDPP DNLAETQKPE QSSLVPGHLD 4400
QVNGQVVPEA SQLSIKQEPR EEPCALGAQS VKREANGEPI GAPGTSNHLL 4450
LAGPRSEAGH LLLQKLLRAK NVQLSTGRGS EGLRAEINGH IDSKLAGLEQ 4500
KLQGTPSNKE DAAARKPLTP KPKRVQKASD RLVSSRKKLR KEDGVRASEA 4550
LLKQLKQELS LLPLTEPAIT ANFSLFAPFG SGCPVNGQSQ LRGAFGSGAL 4600
PTGPDYYSQL LTKNNLSNPP TPPSSLPPTP PPSVQQKMVN GVTPSEELGE 4650
HPKDAASARD SERALRDTSE VKSLDLLAAL PTPPHNQTED VRMESDEDSD 4700
SPDSIVPASS PESILGEEAP RFPHLGSGRW EQEDRALSPV IPLIPRASIP 4750
VFPDTKPYGA LGLEVPGKLP VTTWEKGKGS EVSVMLTVSA AAAKNLNGVM 4800
VAVAELLSMK IPNSYEVLFP ESPARAGTEP KKGEAEGPGG KEKGLEGKSP 4850
DTGPDWLKQF DAVLPGYTLK SQLDILSLLK QESPAPEPPT QHSYTYNVSN 4900
LDVRQLSAPP PEEPSPPPSP LAPSPASPPT EPLVELPTEP LAEPPVPSPL 4950
PLASSPESAR PKPRARPPEE GEDSRPPRLK KWKGVRWKRL RLLLTIQKGS 5000
GRQEDEREVA EFMEQLGTAL RPDKVPRDMR RCCFCHEEGD GATDGPARLL 5050
NLDLDLWVHL NCALWSTEVY ETQGGALMNV EVALHRGLLT KCSLCQRTGA 5100
TSSCNRMRCP NVYHFACAIR AKCMFFKDKT MLCPMHKIKG PCEQELSSFA 5150
VFRRVYIERD EVKQIASIIQ RGERLHMFRV GGLVFHAIGQ LLPHQMADFH 5200
SATALYPVGY EATRIYWSLR TNNRRCCYRC SIGENNGRPE FVIKVIEQGL 5250
EDLVFTDASP QAVWNRIIEP VAAMRKEADM LRLFPEYLKG EELFGLTVHA 5300
VLRIAESLPG VESCQNYLFR YGRHPLMELP LMINPTGCAR SEPKILTHYK 5350
RPHTLNSTSM SKAYQSTFTG ETNTPYSKQF VHSKSSQYRR LRTEWKNNVY 5400
LARSRIQGLG LYAAKDLEKH TMVIEYIGTI IRNEVANRRE KIYEEQNRGI 5450
YMFRINNEHV IDATLTGGPA RYINHSCAPN CVAEVVTFDK EDKIIIISSR 5500
RIPKGEELTY DYQFDFEDDQ HKIPCHCGAW NCRKWMN 5537
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

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. VSP_008560

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51K → N in AAC51734. 1 Publication
Sequence conflicti14 – 141E → Q in AAC51734. 1 Publication
Sequence conflicti75 – 751S → A in AAC51734. 1 Publication
Sequence conflicti156 – 1561E → Q in AAC51734. 1 Publication
Sequence conflicti674 – 948275Missing in AAC51734. 1 PublicationAdd
BLAST
Sequence conflicti1178 – 11781Q → R in AAC51734. 1 Publication
Sequence conflicti1178 – 11781Q → R in AAC51735. 1 Publication
Sequence conflicti1544 – 15474EQAA → DHAP in AAC51734. 1 Publication
Sequence conflicti1544 – 15474EQAA → DHAP in AAC51735. 1 Publication
Sequence conflicti1761 – 17611K → R in AAC51734. 1 Publication
Sequence conflicti1761 – 17611K → R in AAC51735. 1 Publication
Sequence conflicti1766 – 17661D → G in AAC51734. 1 Publication
Sequence conflicti1766 – 17661D → G in AAC51735. 1 Publication
Sequence conflicti2171 – 21711V → A in AAC51734. 1 Publication
Sequence conflicti2171 – 21711V → A in AAC51735. 1 Publication
Sequence conflicti2413 – 24131A → V in AAC51734. 1 Publication
Sequence conflicti2413 – 24131A → V in AAC51735. 1 Publication
Sequence conflicti3079 – 30791K → E in AAC51734. 1 Publication
Sequence conflicti3079 – 30791K → E in AAC51735. 1 Publication
Sequence conflicti3287 – 32871S → P in AAC51734. 1 Publication
Sequence conflicti3287 – 32871S → P in AAC51735. 1 Publication
Sequence conflicti3319 – 33191G → V in AAC51734. 1 Publication
Sequence conflicti3319 – 33191G → V in AAC51735. 1 Publication
Sequence conflicti3422 – 34221D → G in AAC51734. 1 Publication
Sequence conflicti3422 – 34221D → G in AAC51735. 1 Publication
Sequence conflicti4478 – 44781R → Q in AAC51734. 1 Publication
Sequence conflicti4478 – 44781R → Q in AAC51735. 1 Publication
Sequence conflicti4747 – 47471A → D in AAC51734. 1 Publication
Sequence conflicti4747 – 47471A → D in AAC51735. 1 Publication
Sequence conflicti4793 – 47931A → D in AAC51734. 1 Publication
Sequence conflicti4793 – 47931A → D in AAC51735. 1 Publication
Sequence conflicti4826 – 48261A → G in AAC51734. 1 Publication
Sequence conflicti4826 – 48261A → G in AAC51735. 1 Publication
Sequence conflicti4865 – 48651P → A in AAC51734. 1 Publication
Sequence conflicti4865 – 48651P → A in AAC51735. 1 Publication
Sequence conflicti4871 – 48711S → R in AAC51734. 1 Publication
Sequence conflicti4871 – 48711S → R in AAC51735. 1 Publication
Sequence conflicti4893 – 48931S → R in AAC51734. 1 Publication
Sequence conflicti4893 – 48931S → R in AAC51735. 1 Publication
Sequence conflicti4974 – 49741S → T in AAC51734. 1 Publication
Sequence conflicti4974 – 49741S → T in AAC51735. 1 Publication
Sequence conflicti5116 – 51161A → G in AAC51734. 1 Publication
Sequence conflicti5116 – 51161A → G in AAC51735. 1 Publication
Sequence conflicti5522 – 55221K → E in AAC51734. 1 Publication
Sequence conflicti5522 – 55221K → E in AAC51735. 1 Publication

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. 25 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.
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.
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: September 3, 2014
This is version 137 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.

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

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