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Protein

Histone-lysine N-methyltransferase 2B

Gene

Kmt2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2 (By similarity). Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development. Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation.By similarity1 Publication

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 sitei2583 – 25831S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2585 – 25851S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2627 – 26271S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi2653 – 26531ZincBy similarity
Metal bindingi2701 – 27011ZincBy similarity
Binding sitei2702 – 27021S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi2703 – 27031ZincBy similarity
Metal bindingi2708 – 27081ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi37 – 448A.T hook 1
DNA bindingi110 – 1178A.T hook 2
DNA bindingi357 – 3659A.T hook 3
Zinc fingeri964 – 101148CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1207 – 125852PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1255 – 130955PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1341 – 140262PHD-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • gene silencing Source: MGI
  • histone H3-K4 methylation Source: MGI
  • histone H3-K4 trimethylation Source: MGI
  • histone lysine methylation Source: MGI
  • memory Source: MGI
  • oocyte differentiation Source: MGI
  • ovarian follicle development Source: MGI
  • ovulation Source: MGI
  • regulation of histone H3-K4 methylation Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-MMU-3214841. PKMTs methylate histone lysines.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase 2B (EC:2.1.1.43)
Short name:
Lysine N-methyltransferase 2B
Alternative name(s):
Myeloid/lymphoid or mixed-lineage leukemia protein 4 homolog
Trithorax homolog 2
WW domain-binding protein 7
Short name:
WBP-7
Gene namesi
Name:Kmt2b
Synonyms:Mll2, Trx2, Wbp7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:109565. Kmt2b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Females are infertile due to anovulation and follicle loss. Oocytes show reduced H3K4me3 but not H3K4me1, abnormal expression of pro-apoptotic genes and Iap elements (which may contribute to oocyte death and, ultimately, follicle loss) and fail to establish transcriptional repression.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 27132712Histone-lysine N-methyltransferase 2BPRO_0000124882Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei114 – 1141PhosphoserineCombined sources
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei826 – 8261PhosphoserineBy similarity
Modified residuei849 – 8491PhosphoserineBy similarity
Modified residuei866 – 8661PhosphoserineBy similarity
Modified residuei1037 – 10371PhosphoserineCombined sources
Modified residuei1040 – 10401PhosphoserineCombined sources
Modified residuei1098 – 10981PhosphoserineCombined sources
Modified residuei1101 – 11011PhosphoserineCombined sources
Modified residuei1926 – 19261PhosphoserineBy similarity
Modified residuei2064 – 20641PhosphothreonineCombined sources
Modified residuei2079 – 20791PhosphothreonineBy similarity
Modified residuei2346 – 23461PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO08550.
MaxQBiO08550.
PaxDbiO08550.
PRIDEiO08550.

PTM databases

iPTMnetiO08550.
PhosphoSiteiO08550.

Expressioni

Gene expression databases

BgeeiO08550.
CleanExiMM_WBP7.
ExpressionAtlasiO08550. baseline and differential.
GenevisibleiO08550. MM.

Interactioni

Subunit structurei

Component of the menin-associated histone methyltransferase complex, at least composed of KMT2B/MLL4, ASH2L, RBBP5, WDR5, DPY30, MEN1; the complex interacts with POLR2A and POLR2B via MEN1. Interacts with NFE2. Interacts with KDM6B.By similarity

Protein-protein interaction databases

BioGridi217461. 3 interactions.
IntActiO08550. 1 interaction.
MINTiMINT-1525361.
STRINGi10090.ENSMUSP00000103789.

Structurei

3D structure databases

ProteinModelPortaliO08550.
SMRiO08550. Positions 961-1021, 1360-1399, 2539-2713.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1733 – 178957FYR N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2409 – 249082FYR C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2573 – 2689117SETPROSITE-ProRule annotationAdd
BLAST
Domaini2697 – 271317Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2650 – 26512S-adenosyl-L-methionine bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 106101Gly-richAdd
BLAST
Compositional biasi272 – 30029Gly-richAdd
BLAST
Compositional biasi347 – 41064Glu-richAdd
BLAST
Compositional biasi414 – 776363Pro-richAdd
BLAST
Compositional biasi1814 – 2296483Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation
Contains 3 A.T hook DNA-binding domains.Curated
Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
Contains 1 FYR C-terminal domain.PROSITE-ProRule annotation
Contains 1 FYR N-terminal domain.PROSITE-ProRule annotation
Contains 3 PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri964 – 101148CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1207 – 125852PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1255 – 130955PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1341 – 140262PHD-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1084. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00760000119228.
HOGENOMiHOG000015326.
HOVERGENiHBG100043.
InParanoidiO08550.
KOiK14959.
TreeFamiTF319820.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR002857. Znf_CXXC.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTiSM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00249. PHD. 4 hits.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. 3 hits.
PS50016. ZF_PHD_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O08550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAGGGSC PGPGSARGRF PGRPRGSGGG GGRGGRGNGA ERVRVALRRG
60 70 80 90 100
GGAAGPGGAE PGEDTALLRL LGLRRGLRRL RRLWAGARVQ RGRGRGRGRG
110 120 130 140 150
WGPNRGCMPE EESSDGESEE EEFQGFHSDE DVAPSSLRSA LRSQRGRAPR
160 170 180 190 200
GRGRKHKTTP LPPRLADVTP VPPKAPTRKR GEEGTERMVQ ALTELLRRSQ
210 220 230 240 250
APQPPRSRAR AREPSTPRRS RGRPPGRPAG PCRKKQQAVV LAEAAVTIPK
260 270 280 290 300
PEPPPPVVPV KNKAGSWKCK EGPGPGPGTP KRGGQPGRGG RGGRGRGRGG
310 320 330 340 350
LPLMIKFVSK AKKVKMGQLS QELESGQGHG QRGESWQDAP QRKDGDEPER
360 370 380 390 400
GSCRKKQEQK LEEEEEEEEK EGEEKEEKDD NEDNNKQEEE EETERAVAEE
410 420 430 440 450
EAMLAKEKEE AKLPSPPLTP PVPSPPPPLP PPSTSPPPPA SPLPPPVSPP
460 470 480 490 500
PPLSPPPYPA PEKQEESPPL VPATCSRKRG RPPLTPSQRA EREAARSGPE
510 520 530 540 550
GTLSPTPNPS TTTGSPLEDS PTVVPKSTTF LKNIRQFIMP VVSARSSRVI
560 570 580 590 600
KTPRRFMDED PPKPPKVEAS IVRPPVATSP PAPQEPVPVS SPPRVPTPPS
610 620 630 640 650
TPVPLPEKRR SILREPTFRW TSLTRELPPP PPAPPPAPSP PPAPATPSRR
660 670 680 690 700
PLLLRAPQFT PSEAHLKIYE SVLTPPPLGA LETPEPELPP ADDSPAEPEP
710 720 730 740 750
RAVGRTNHLS LPRFVPVVTS PVKVEVPPHG APALSEGQQL QLQQPPQALQ
760 770 780 790 800
TQLLPQALPP QQPQAQPPPS PQHTPPLEKA RVASLGSLPL SGVEEKMFSL
810 820 830 840 850
LKRAKVQLFK IDQQQQQKVA ASMPLSPAVQ TEEAVGTVKQ TPDRGCVRSE
860 870 880 890 900
DESMEAKRDR ASGPESPLQG PRIKHVCRHA AVALGQARAM VPEDVPRLSA
910 920 930 940 950
LPLRDRQDLA TEDTSSASET ESVPSRSQRE KVESAGPGGD SEPTGSTGAL
960 970 980 990 1000
AHTPRRSLPS HHGKKMRMAR CGHCRGCLRV QDCGSCVNCL DKPKFGGPNT
1010 1020 1030 1040 1050
KKQCCVYRKC DKIEARKMER LAKKGRTIVK TLLPWDSDES PEASPGPPGP
1060 1070 1080 1090 1100
RRGAGAGGSR EEVGATPGPE EQDSLLLQRK SARRCVKQRP SYDVFEDSDD
1110 1120 1130 1140 1150
SEPGGPPAPR RRTPREHELP VLEPEEQSRP RKPTLQPVLQ LKARRRLDKD
1160 1170 1180 1190 1200
ALAPGPFASF PNGWTGKQKS PDGVHRVRVD FKEDCDLENV WLMGGLSVLT
1210 1220 1230 1240 1250
SVPGGPPMVC LLCASKGLHE LVFCQVCCDP FHPFCLEEAE RPSPQHRDTW
1260 1270 1280 1290 1300
CCRRCKFCHV CGRKGRGSKH LLECERCRHA YHPACLGPSY PTRATRRRRH
1310 1320 1330 1340 1350
WICSACVRCK SCGATPGKNW DVEWSGDYSL CPRCTELYEK GNYCPICTRC
1360 1370 1380 1390 1400
YEDNDYESKM MQCAQCDHWV HAKCEGLSDE DYEILSGLPD SVLYTCGPCA
1410 1420 1430 1440 1450
GATQPRWREA LSGALQGGLR QVLQGLLSSK VAGPLLLCTQ CGQDGKQLHP
1460 1470 1480 1490 1500
GPCDLQAVGK RFEEGLYKSV HSFMEDVVAI LMRHSEEGET PERRAGSQMK
1510 1520 1530 1540 1550
GLLLKLLESA FCWFDAHDPK YWRRSTRLPN GVLPNAVLPP SLDHVYAQWR
1560 1570 1580 1590 1600
QQESETPESG QPPGDPSAAF QSKDPAAFSH LDDPRQCALC LKYGDADSKE
1610 1620 1630 1640 1650
AGRLLYIGQN EWTHVNCAIW SAEVFEENDG SLKNVHAAVA RGRQMRCELC
1660 1670 1680 1690 1700
LKPGATVGCC LSSCLSNFHF MCARASYCIF QDDKKVFCQK HTDLLDGKEI
1710 1720 1730 1740 1750
VTPDGFDVLR RVYVDFEGIN FKRKFLTGLE PDVINVLIGS IRINSLGTLS
1760 1770 1780 1790 1800
DLSDCEGRLF PIGYQCSRLY WSTVDARRRC WYRCRILEYR PWGPREEPVH
1810 1820 1830 1840 1850
LEAAEENQTI VHSPTPSSDT DSLIPGDPVH HSPIQNLDPP LRTDSSNGPP
1860 1870 1880 1890 1900
PTPRSFSGAR IKVPNYSPSR RPLGGVSFGP LPSPGSPSSL THHIPTVGDS
1910 1920 1930 1940 1950
DFPAPPRRSR RPSPLATRPP PSRRTSSPLR TSPQLRVPLS TSVTALTPTS
1960 1970 1980 1990 2000
GELAPPDLAP SPLPPSEDLG PDFEDMEVVS GLSAADLDFA ASLLGTEPFQ
2010 2020 2030 2040 2050
EEIVAAGAVG SSQGGPGDSS EEEASPTTHY VHFPVTVVSG PALAPSSLAG
2060 2070 2080 2090 2100
APRIEQLDGV DDGTDSEAEA VQQPRGQGTP PSGPGVGRGG VLGAAGDRAQ
2110 2120 2130 2140 2150
PPEDLPSEIV DFVLKNLGGP GEGAAGPRED SLPSAPPLAN GSQPPQSLST
2160 2170 2180 2190 2200
SPADPTRTFA WLPGAPGVRV LSLGPAPEPP KPATSKIILV NKLGQVFVKM
2210 2220 2230 2240 2250
AGEGEPVAPP VKQPPLPPII PPTAPTSWTL PPGPLLSVLP VVGVGVVRPA
2260 2270 2280 2290 2300
PPPPPPPLTL VFSSGPPSPP RQAIRVKRVS TFSGRSPPVP PPNKTPRLDE
2310 2320 2330 2340 2350
DGESLEDAHH VPGISGSGFS RVRMKTPTVR GVLDLNNPGE QPEEESPGRP
2360 2370 2380 2390 2400
QDRCPLLPLA EAPSQALDGS SDLLFESQWH HYSAGEASSS EEEPPSPEDK
2410 2420 2430 2440 2450
ENQVPKRVGP HLRFEISSDD GFSVEAESLE VAWRTLIEKV QEARGHARLR
2460 2470 2480 2490 2500
HLSFSGMSGA RLLGIHHDAV IFLAEQLPGA QRCQHYKFRY HQQGEGQEEP
2510 2520 2530 2540 2550
PLNPHGAARA EVYLRKCTFD MFNFLASQHR VLPEGATCDE EEDEVQLRST
2560 2570 2580 2590 2600
RRATSLELPM AMRFRHLKKT SKEAVGVYRS AIHGRGLFCK RNIDAGEMVI
2610 2620 2630 2640 2650
EYSGIVIRSV LTDKREKFYD GKGIGCYMFR MDDFDVVDAT MHGNAARFIN
2660 2670 2680 2690 2700
HSCEPNCFSR VIHVEGQKHI VIFALRRILR GEELTYDYKF PIEDASNKLP
2710
CNCGAKRCRR FLN
Length:2,713
Mass (Da):294,821
Last modified:July 27, 2011 - v3
Checksum:i2AD4343C5C081933
GO

Sequence cautioni

The sequence AAC53192.1 differs from that shown.Possible contaminating sequence. The N-terminal 3 residues and C-terminal 8 residues do not match the underlying genomic sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181G → V in BAD81031 (Ref. 1) Curated
Sequence conflicti25 – 273RGS → LGC in BAD81031 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB182318 mRNA. Translation: BAD81031.1.
AC167970 Genomic DNA. No translation available.
U92455 mRNA. Translation: AAC53192.1. Sequence problems.
CCDSiCCDS21101.1.
RefSeqiNP_083550.2. NM_029274.2.
UniGeneiMm.168688.

Genome annotation databases

EnsembliENSMUST00000108154; ENSMUSP00000103789; ENSMUSG00000006307.
GeneIDi75410.
KEGGimmu:75410.
UCSCiuc009gfg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB182318 mRNA. Translation: BAD81031.1.
AC167970 Genomic DNA. No translation available.
U92455 mRNA. Translation: AAC53192.1. Sequence problems.
CCDSiCCDS21101.1.
RefSeqiNP_083550.2. NM_029274.2.
UniGeneiMm.168688.

3D structure databases

ProteinModelPortaliO08550.
SMRiO08550. Positions 961-1021, 1360-1399, 2539-2713.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217461. 3 interactions.
IntActiO08550. 1 interaction.
MINTiMINT-1525361.
STRINGi10090.ENSMUSP00000103789.

PTM databases

iPTMnetiO08550.
PhosphoSiteiO08550.

Proteomic databases

EPDiO08550.
MaxQBiO08550.
PaxDbiO08550.
PRIDEiO08550.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108154; ENSMUSP00000103789; ENSMUSG00000006307.
GeneIDi75410.
KEGGimmu:75410.
UCSCiuc009gfg.1. mouse.

Organism-specific databases

CTDi9757.
MGIiMGI:109565. Kmt2b.

Phylogenomic databases

eggNOGiKOG1084. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00760000119228.
HOGENOMiHOG000015326.
HOVERGENiHBG100043.
InParanoidiO08550.
KOiK14959.
TreeFamiTF319820.

Enzyme and pathway databases

ReactomeiR-MMU-3214841. PKMTs methylate histone lysines.

Miscellaneous databases

NextBioi342938.
PROiO08550.
SOURCEiSearch...

Gene expression databases

BgeeiO08550.
CleanExiMM_WBP7.
ExpressionAtlasiO08550. baseline and differential.
GenevisibleiO08550. MM.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR002857. Znf_CXXC.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTiSM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00249. PHD. 4 hits.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. 3 hits.
PS50016. ZF_PHD_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Murine MLL2 gene and its expression."
    Yoshida K.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands."
    Bedford M.T., Chan D.C., Leder P.
    EMBO J. 16:2376-2383(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 379-657.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-114; SER-118; SER-1037; SER-1040; SER-1098; SER-1101; THR-2064 AND SER-2346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Spleen and Testis.
  6. "MLL2 is required in oocytes for bulk histone 3 lysine 4 trimethylation and transcriptional silencing."
    Andreu-Vieyra C.V., Chen R., Agno J.E., Glaser S., Anastassiadis K., Stewart A.F., Matzuk M.M.
    PLoS Biol. 8:1657-1680(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiKMT2B_MOUSE
AccessioniPrimary (citable) accession number: O08550
Secondary accession number(s): E9QKF4, Q5NU09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

The human ortholog, KMT2B/MLL4, was first named MLL2 (see AC Q9UMN6). Thus, mouse Kmt2b/Mll4 is also 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.