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Q6PDK2

- KMT2D_MOUSE

UniProt

Q6PDK2 - KMT2D_MOUSE

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Protein

Histone-lysine N-methyltransferase 2D

Gene

Kmt2d

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei5502 – 55021S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi5528 – 55281ZincBy similarity
Metal bindingi5576 – 55761ZincBy similarity
Metal bindingi5578 – 55781ZincBy similarity
Metal bindingi5583 – 55831ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri226 – 27651PHD-type 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 27446RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri270 – 32354PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri276 – 32146RING-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1071 – 112454PHD-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1121 – 117151PHD-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1198 – 125356PHD-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1201 – 125151RING-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4829 – 487446RING-type 4; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
  2. 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: MGI
  4. oocyte growth Source: UniProtKB
  5. oogenesis Source: UniProtKB
  6. 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_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_219771. deactivation of the beta-catenin 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:Mll2, Mll4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:2682319. Kmt2d.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 55885588Histone-lysine N-methyltransferase 2DPRO_0000401938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1562 – 15621PhosphoserineBy similarity
Modified residuei1627 – 16271Phosphoserine1 Publication
Modified residuei2203 – 22031N6-acetyllysineBy similarity
Modified residuei2231 – 22311PhosphoserineBy similarity
Modified residuei2266 – 22661PhosphoserineBy similarity
Modified residuei2268 – 22681PhosphoserineBy similarity
Modified residuei3071 – 30711N6-acetyllysine1 Publication
Modified residuei3122 – 31221PhosphoserineBy similarity
Modified residuei3193 – 31931PhosphoserineBy similarity
Modified residuei3430 – 34301N6-acetyllysineBy similarity
Modified residuei4272 – 42721PhosphoserineBy similarity
Modified residuei4410 – 44101PhosphoserineBy similarity
Modified residuei4516 – 45161N6-acetyllysineBy similarity
Modified residuei4789 – 47891Phosphoserine1 Publication
Modified residuei4827 – 48271N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ6PDK2.
PaxDbiQ6PDK2.
PRIDEiQ6PDK2.

PTM databases

PhosphoSiteiQ6PDK2.

Expressioni

Gene expression databases

BgeeiQ6PDK2.
ExpressionAtlasiQ6PDK2. baseline and differential.
GenevestigatoriQ6PDK2.

Interactioni

Subunit structurei

Interacts with ESR1; interaction is direct (By similarity). 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.By similarity1 Publication

Protein-protein interaction databases

BioGridi237747. 15 interactions.
IntActiQ6PDK2. 2 interactions.
STRINGi10090.ENSMUSP00000023741.

Structurei

3D structure databases

ProteinModelPortaliQ6PDK2.
SMRiQ6PDK2. Positions 220-323, 1957-2034.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati442 – 44651
Repeati460 – 46452
Repeati469 – 47354
Repeati477 – 48155
Repeati520 – 52457
Repeati529 – 53358
Repeati538 – 54259
Repeati547 – 551510
Repeati574 – 578511
Repeati583 – 587512
Repeati592 – 596513
Repeati610 – 614514
Repeati637 – 641515
Domaini5226 – 528661FYR N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini5287 – 537286FYR C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini5448 – 5564117SETPROSITE-ProRule annotationAdd
BLAST
Domaini5572 – 558817Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni439 – 64220415 X 5 AA repeats of S/P-P-P-E/P-E/AAdd
BLAST
Regioni5525 – 55262S-adenosyl-L-methionine bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2627 – 266539Sequence AnalysisAdd
BLAST
Coiled coili2768 – 281346Sequence AnalysisAdd
BLAST
Coiled coili3559 – 361355Sequence AnalysisAdd
BLAST
Coiled coili3712 – 374736Sequence AnalysisAdd
BLAST
Coiled coili3854 – 388330Sequence AnalysisAdd
BLAST
Coiled coili3912 – 4052141Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2644 – 26485LXXLL motif 1
Motifi3030 – 30345LXXLL motif 2
Motifi4279 – 429315LXXLL motif 3Add
BLAST
Motifi4310 – 43145LXXLL motif 4
Motifi4514 – 45185LXXLL motif 5
Motifi5041 – 50455LXXLL motif 6

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1307 – 13115Poly-Glu
Compositional biasi2064 – 2583520Pro-richAdd
BLAST
Compositional biasi2610 – 26134Poly-Ser
Compositional biasi2769 – 281244Gln-richAdd
BLAST
Compositional biasi2813 – 28197Poly-Ala
Compositional biasi3255 – 43321078Gln-richAdd
BLAST
Compositional biasi4841 – 48444Poly-Ala
Compositional biasi4960 – 502869Pro-richAdd
BLAST

Domaini

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

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 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 27446RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri270 – 32354PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri276 – 32146RING-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1071 – 112454PHD-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1121 – 117151PHD-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1198 – 125356PHD-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1201 – 125151RING-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4829 – 487446RING-type 4; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000119228.
HOGENOMiHOG000168503.
InParanoidiQ6PDK2.
PhylomeDBiQ6PDK2.

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. 4 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6PDK2-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MDSQKPPAED KDSDPAADGL AAPEKPGATE PDLPILCIGE VSVPGSGGSR
60 70 80 90 100
PQKPPHDCSR GPARRCALCN CGEPGLHGQR ELQRFELPSD WPGFPVVPSG
110 120 130 140 150
GNSGPCEAVL PKEDASQIGF PEGLTPAHLG EPGGHCWAHH WCAAWSAGVW
160 170 180 190 200
GQEGPELCGV DKAIFSGISQ RCSHCARFGA SVPCRSPGCS RLYHFPCATA
210 220 230 240 250
SGSFLSMKTL QLLCPEHSDG AAHLEEARCA VCEGPGQLCD LLFCTSCGHH
260 270 280 290 300
YHGACLDTAL TARKRASWQC PECKVCQSCR KPGNDSKMLV CETCDKGYHT
310 320 330 340 350
FCLKPPMEDL PAHSWKCKTC RLCRACGAGS AELNPNSEWF ENYSLCHRCH
360 370 380 390 400
KAQGSQPVTS VAEQHPAVCS RLSPPEPGEI PIDAPDALYV ACQGQPKGGH
410 420 430 440 450
VTSMQPKELA PLQCEAKPLG RAGTQLEAQL EAPLHEEMPL LPPPEESPLS
460 470 480 490 500
PPPEESPTSP PPEASRLSPP TEESPLSPPP ESSPFSPLEG CPPSPALDTP
510 520 530 540 550
LSPPPEASPL SPPFEESPLS PPPEELPSSP PPEASRLSPP PEESPMSPPP
560 570 580 590 600
EESPMSPPPE ASRLFPPFEE SPLSPPPEDS PLSPPPEASR LSPPPEDSPM
610 620 630 640 650
SPPPEDSPMS PPPEVSRFLP LPVLSHLSPL PEVSRLSPPP EESPLSPPPE
660 670 680 690 700
DSPASPPPEA SRLSPPPEDS PASPPPEASR LSRPREDSPA SPPPEDSLVS
710 720 730 740 750
LPMEESPLSP LPEELRLCPQ PEEPYLSPQP EEPRLCPQPE ELPLSPQSEE
760 770 780 790 800
PCLSPVLVEP GPSSQPEEPH LSPVPQEPHL SPQPEEPHLS PQPQQLHLSP
810 820 830 840 850
HSEEPCLSPM PEEPCLSPQP EELNGPPQPA EPPEEPSQSS APKELSLFSP
860 870 880 890 900
SGEPPLPPML GEPALSEPGE PPLSPLPEEL PLSLSGEPVL SPQLMPPDPL
910 920 930 940 950
PPPLSPIIPA AAPPALSPLG ELEYPFGAKG DSDPESPLAA PILETPISPP
960 970 980 990 1000
PEANCTDPEP VPPMILPPSP GSPLGPASPI LMERLPPPCS PLLPHSLPPP
1010 1020 1030 1040 1050
TPPPSHCSPP ALPLSVPSPL SPVQKAVDVS DEAELHEMET DKGPEPECPA
1060 1070 1080 1090 1100
LEPRATSPLP SPLGDLSCPA PSPAPALDDF SGLGEDTAPL DGTGQMSGSL
1110 1120 1130 1140 1150
AGELKGSPVL LDPEELTPVT PMEVYGPECK QAGQGSPCEE QEEPGAPMAP
1160 1170 1180 1190 1200
MPPTLIKSDI VNEISNLSQG DASASFPGSE PLLGSPDPEG GGSLSMELGV
1210 1220 1230 1240 1250
STDVSPARDE GSLRLCTDSL PETDDSLLCD TGTATSGGKA EGDKGRRRSS
1260 1270 1280 1290 1300
PARSRIKQGR SSSFPGRRRP RGGAAHGGRG RGRARLKSTT SSVETLVADI
1310 1320 1330 1340 1350
DSSPSKEEEE EDDDTMQNTV VLFSNTDKFV LMQDMCVVCG SFGRGAEGHL
1360 1370 1380 1390 1400
LACSQCSQCY HPYCVNSKIT KVMLLKGWRC VECIVCEVCG QASDPSRLLL
1410 1420 1430 1440 1450
CDDCDISYHT YCLDPPLLTV PKGGWKCKWC VSCMQCGAAS PGFHCEWQNS
1460 1470 1480 1490 1500
YTHCGPCASL VTCPVCHAPY VEEDLLIQCR HCERWMHAGC ESLFTEDEVE
1510 1520 1530 1540 1550
QAADEGFDCV SCQPYVVKPV VPVAPPELVP VKVKEPEPQF FRFEGVWLTE
1560 1570 1580 1590 1600
TGMAVLRNLT MSPLHKRRQR RGRLGLPGEA GLEGSEPSDA LGPDDKKDGD
1610 1620 1630 1640 1650
LDTDDLLKGE GGVEQMECEI KLEGPASPDV ELGKEETEES KKRKRKPYRP
1660 1670 1680 1690 1700
GIGGFMVRQR KSHTRVKRGP AAQAEVLSGD GQPDEVMPAD LPAEGSVEQS
1710 1720 1730 1740 1750
LAEGDEKKKQ QRRARKKSKL EDMFPAYLQA AFFGKDLLDL SRKALFAVGV
1760 1770 1780 1790 1800
GRPGFGLGAS KPRADGGSDR KELMTAMHKG DDGPDVADEE SHGPEGTADL
1810 1820 1830 1840 1850
PGLEDGGVKA SPVPSDPEKP GTPGEGVLSS DLDRIPTEEL PKMESKDLQQ
1860 1870 1880 1890 1900
LFKDVLGSER EQHLGCGTPG LEGGRTSLQR PFLQGGLALG SLPSSSPMDS
1910 1920 1930 1940 1950
YPGLCQSPFL DSRERGGFFS PEPGEPDSPW TGSGGTTPST PTTPTTEGEG
1960 1970 1980 1990 2000
DGLSYNQRSL QRWEKDEELG QLSTISPVLY ANINFPNLKQ DYPDWSSRCK
2010 2020 2030 2040 2050
QIMKLWRKVP AADKAPYLQK AKDNRAAHRI SKVQKQAESQ ISKQAKMGDI
2060 2070 2080 2090 2100
ARKTDRPALH LRIPSQPGAL GSPPPAAAPT IFLGSPTTPA GLSTSADGFL
2110 2120 2130 2140 2150
KPPAGTVPGP DSPGELFLKL PPQVPAQVPS QDPFGLAPAY APEPRFSAAP
2160 2170 2180 2190 2200
PTYPPYPSPT GAPAQPPMLG TTTRPGTGQP GEFHTTPPGT PRHQPSTPDP
2210 2220 2230 2240 2250
FLKPRCPSLD NLAVPESPGV AGGKASEPLL SPPPFGESRK SLEVKKEELG
2260 2270 2280 2290 2300
ASSPGYGPPN LGCVDSPSAG PHLGGLELKA PDVFKAPLTP RASQVEPQSP
2310 2320 2330 2340 2350
GLGLRAQEPP PAQALAPSPP SHPDVFRSGP YPDPYAQPPL TPRPQPPPPE
2360 2370 2380 2390 2400
SCCAPPPRSL PSDPFSRVPA SPQSQSSSQS PLTPRPLSAE AFCPSPVTPR
2410 2420 2430 2440 2450
FQSPDPYSRP PSRPQSRDPF APLHKPPRPQ PPEVAFKAGP LAHTPLGAGG
2460 2470 2480 2490 2500
FPAALPSGPA GELHAKVPSG QPTNFARSPG TGTFVGTPSP MRFTFPQGVG
2510 2520 2530 2540 2550
EPSLKPPVPQ PGLPSPHGIN SHFGPGPTLG KPQSTNYAVA TGNFHPSGSP
2560 2570 2580 2590 2600
LGPNSGPTGE GYGLSPLRPA SVLPPPAPDG SLPYLTHGAS QRVGITSPVE
2610 2620 2630 2640 2650
KREDPGATMS SSSLATPELS SAQDAGISSL SQTELEKQRQ RQRLRELLIR
2660 2670 2680 2690 2700
QQIQRNTLRQ EKETAAAAAG AVGPPGNWGA EPSSPAFEQL SRGQTPFTGS
2710 2720 2730 2740 2750
QDRSSIVGLP ASKLGGPTLG PGAFSSDDRL ARPLPPATPS SMDMNSRQLV
2760 2770 2780 2790 2800
GGSQAFYQRT PYPGSLPLQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQLWQ
2810 2820 2830 2840 2850
QQQQQQQQQQ QQAAAAAAAT SMRLAMSARF PSTPGPELGR QALGSPLAGI
2860 2870 2880 2890 2900
PTRLPGPAEP VPGPAGPAQF IELRHNVQKG LGPGVSPFPG QGPPQRPRFY
2910 2920 2930 2940 2950
PVSEELHRLA PEGLRGLAVP GLPSQKPSAL PAPELNNSLH QTPHAKGPAL
2960 2970 2980 2990 3000
ASGLELVSRP PSNTELSRPP LALEAGKLPC EDPELDDDFD AHKALEDDEE
3010 3020 3030 3040 3050
LAHLGLGVDV AKGDDELGTL ENLETNDPHL DDLLNGDEFD LLAYTDPELD
3060 3070 3080 3090 3100
TGDKKDIFNE HLRLVESANE KAEREALLRG VEPVSLGPEE RPPPAPDNSE
3110 3120 3130 3140 3150
PRLTSVLPEV KPKVEEGGRH PSPCQFTINT PKVEPAPPAT SLSLGLKPGQ
3160 3170 3180 3190 3200
TVMGTRDTRG GVGTGSFPSS GHTAEKGPFG ATGGTPAHLL NPSSLSGPAA
3210 3220 3230 3240 3250
SSLLEKFELE SGALTLPSGH AAAGDELDKM ESSLVASELP LLIEDLLEHE
3260 3270 3280 3290 3300
KKELQKKQQL SAQTVLPAQQ QQQQQQQQQQ QQQQHTLLPT PGPAQALPLP
3310 3320 3330 3340 3350
HEPGPPQQLA LGIGSTRQPG LGQSMVPIQP PAHALQQRLA PSVAMVSNQG
3360 3370 3380 3390 3400
HMLSGQQAGQ TGLVPQQSSQ PVLAQKPMSA MPASMCMKPQ QLAMQQQQLA
3410 3420 3430 3440 3450
NSFFPDTDLD KFAAEDIIDP IAKAKMVALK GIKKVMAQGS IGVAPGMNRQ
3460 3470 3480 3490 3500
QVSLLAQRLS GGSGSDLQNH VAPGSGQERN AGDPAQPRPN PPTFAQGVIN
3510 3520 3530 3540 3550
EADQRQYEEW LFHTQQLLQM QLKVLEEQIG VHRKSRKALC AKQRTAKKAG
3560 3570 3580 3590 3600
REFPEADAEK LKLVTEQQSK IQKQLDQVRK QQKEHTNLMA EYRNKQQQQQ
3610 3620 3630 3640 3650
QQQQQQQQQQ HSAVLAVSPS QNPRVLTKLP GQLLPAHGLQ PPQAPPGGQA
3660 3670 3680 3690 3700
GGLRLPPGGM VLPGQSGGPF LNTTLAQQQQ QQHSGVAGSL TGPPGSFFPG
3710 3720 3730 3740 3750
NLALRSLGPD SRLLQERQLQ LQQQRMQLAQ KLQQQQQQQQ QQQQQQHLLG
3760 3770 3780 3790 3800
QVAIQQQQGP GVQNQALGPK PQGLLPPSNH QGLLVQQLSP QQSQGSQGLL
3810 3820 3830 3840 3850
GPAQVTVLQQ QQQQQQHSGA LGPQGPHRQV LMTQSRVLSS PQLAQQGHSL
3860 3870 3880 3890 3900
MGHRLLTAQQ QQQQQQQQQQ QQQQQQQQQQ QQQGSMTGLS QLQQGMMSHG
3910 3920 3930 3940 3950
GQPKMSAQAL GSLQQQQQQL QQQQMLQQQQ LQQQQQQLQQ QQQQQQLQQQ
3960 3970 3980 3990 4000
QQQQLQLQQQ QQQQQQHLQH QQQQQQQLQQ QQQLQQQQQQ QLHLQQQLHQ
4010 4020 4030 4040 4050
QQQLQLQQQQ MGLLNQNRTL LSPQQQQQQQ QQQQQQQQQQ QQQQQQQQQV
4060 4070 4080 4090 4100
TLGPGLPVKP LQHFSSSGAL GPTLLLTGKE QNNAETALPS EVTEGPSTHQ
4110 4120 4130 4140 4150
GGPPAVGTAP EPMSVEPGEV KPSISGDSQL LLVQSQAQSQ ATSVQLQPPL
4160 4170 4180 4190 4200
RLPGQPQPQV NLLHTAGGGS HGQQLGSGSS SESPAVPHLL AQPSVSLGEQ
4210 4220 4230 4240 4250
PGPMAQNLLG SQQPLGLDRP IQNNTGSQPP KSGPAPQSGQ GPPGAGVMPT
4260 4270 4280 4290 4300
VGQLRAQLQG VLAKNPQLRH LSPQQQQQLQ ALLMQRQLQQ SQAVRQTPPF
4310 4320 4330 4340 4350
QEPGTQPSPL QGLLGCQPQP GGFSVSQTGP LQELGAGSRP QGPPRLPVPQ
4360 4370 4380 4390 4400
GALSTGPVLG PAHPTPPPSS PQEPKRPSQL PSPSAQLTPT HPGTPKPQGP
4410 4420 4430 4440 4450
ALELPPGRVS PAAAQLADTF FGKGLGPWDP SDNLTEAQKP EQSSLVPGHL
4460 4470 4480 4490 4500
DQVNGQVVHE PSQLSIKQEP REEPCALGAQ TVKREANGEP AGAPGTSNHL
4510 4520 4530 4540 4550
LLAGSRSEAG HLLLQKLLRA KNVQLGAGRG PEGLRAEING HIDSKLSGLE
4560 4570 4580 4590 4600
QKLQGTSSNK EDAATRKPLP AKPKRVQKTS DRLPSSRKKL RKEDGVRANE
4610 4620 4630 4640 4650
ALLKQLKQEL SQLPLTEPTI TANFSLFAPF GSGCLVSGQS QLRGAFGSGA
4660 4670 4680 4690 4700
LHTGPDYYSQ LLTKNNLSNP PTPPSSLPPT PPPSVQQKMV NGVTPSDELG
4710 4720 4730 4740 4750
ERPKDTASAQ DSEGALRDAA EVKSLDLLAA LPTPPHNQTE DVRMESDEDS
4760 4770 4780 4790 4800
DSPDSIVPAS SPESILGEEA PRFPQLGSGR WEQDNRALSP VIPIIPRTGI
4810 4820 4830 4840 4850
PVFPDTKPYG VLDLEVPGKL PATAWEKGKG SEVSVMLTVS AAAAKNLNGV
4860 4870 4880 4890 4900
MVAVAELLSM KIPNSYEVLF PDGPARAGLE PKKGEAEGPG GKEKGLSGKG
4910 4920 4930 4940 4950
PDTGPDWLKQ FDAVLPGYTL KSQLDILSLL KQESPAPEPS IQHSYTYNVS
4960 4970 4980 4990 5000
NLDVRQLSAP PPEEPSPPPS PLAPSPASPP AEPMVELQAE RPAEPPIPSP
5010 5020 5030 5040 5050
LPLASSPESA RPKPRARPPE ESEDSRPPRL KKWKGVRWKR LRLLLTIQKG
5060 5070 5080 5090 5100
SGHQEDEREV AEFMEQFGTA LRPSKVPRDN RRCCFCHEEG DGATDGPARL
5110 5120 5130 5140 5150
LNLDLDLWVH LNCALWSTEV YETQGGALMN VEVALHRGLL TKCSLCQRTG
5160 5170 5180 5190 5200
ATSSCNRMRC PNVYHFACAI RAKCMFFKDK TMLCPVHKIK GPCEQELSSF
5210 5220 5230 5240 5250
AVFRRVYIER DEVKQIASII QRGERLHMFR VGGLVFHAIG QLLPHQMADF
5260 5270 5280 5290 5300
HSATALYPVG YEATRIYWSL RTNNRRCCYR CSISENNGRP EFVIKVIEQG
5310 5320 5330 5340 5350
LEDLVFTDAS PQAVWNRIIE PVAAMRKEAD MLRLFPEYLK GEELFGLTVH
5360 5370 5380 5390 5400
AVLRIAESLP GVESCQNYLF RYGRHPLMEL PLMINPTGCA RSEPKILTHY
5410 5420 5430 5440 5450
KRPHTLNSTS MSKAYQSTFT GETNTPYSKQ FVHSKSSQYR RLRTEWKNNV
5460 5470 5480 5490 5500
YLARSRIQGL GLYAAKDLEK HTMVIEYIGT IIRNEVANRR EKIYEEQNRG
5510 5520 5530 5540 5550
IYMFRINNEH VIDATLTGGP ARYINHSCAP NCVAEVVTFD KEDKIIIISS
5560 5570 5580
RRIPKGEELT YDYQFDFEDD QHKIPCHCGA WNCRKWMN
Length:5,588
Mass (Da):600,245
Last modified:November 30, 2010 - v2
Checksum:i37A0E5D319A5F1A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC161165 Genomic DNA. No translation available.
BC058659 mRNA. Translation: AAH58659.1.
CCDSiCCDS49725.2.
UniGeneiMm.264889.

Genome annotation databases

EnsembliENSMUST00000178486; ENSMUSP00000135941; ENSMUSG00000048154.
UCSCiuc029suy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC161165 Genomic DNA. No translation available.
BC058659 mRNA. Translation: AAH58659.1 .
CCDSi CCDS49725.2.
UniGenei Mm.264889.

3D structure databases

ProteinModelPortali Q6PDK2.
SMRi Q6PDK2. Positions 220-323, 1957-2034.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 237747. 15 interactions.
IntActi Q6PDK2. 2 interactions.
STRINGi 10090.ENSMUSP00000023741.

PTM databases

PhosphoSitei Q6PDK2.

Proteomic databases

MaxQBi Q6PDK2.
PaxDbi Q6PDK2.
PRIDEi Q6PDK2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000178486 ; ENSMUSP00000135941 ; ENSMUSG00000048154 .
UCSCi uc029suy.1. mouse.

Organism-specific databases

MGIi MGI:2682319. Kmt2d.

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00760000119228.
HOGENOMi HOG000168503.
InParanoidi Q6PDK2.
PhylomeDBi Q6PDK2.

Enzyme and pathway databases

Reactomei REACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_219771. deactivation of the beta-catenin transactivating complex.

Miscellaneous databases

PROi Q6PDK2.
SOURCEi Search...

Gene expression databases

Bgeei Q6PDK2.
ExpressionAtlasi Q6PDK2. baseline and differential.
Genevestigatori Q6PDK2.

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. 4 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4339-5588.
    Strain: C57BL/6.
    Tissue: Brain.
  3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4789, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1627, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains."
    Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.
    Cell 144:513-525(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL COMPLEX, INTERACTION WITH ASH2L; DPY30; KMT2A; RRBP5 AND WDR5.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiKMT2D_MOUSE
AccessioniPrimary (citable) accession number: Q6PDK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: November 30, 2010
Last modified: November 26, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Human protein KMT2B/MLL4 was first named MLL2 (see AC Q9UMN6). Thus, also mouse Mll4 is often referred to as Mll2 and vice versa in the literature.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3