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Protein

Histone-lysine N-methyltransferase 2B

Gene

KMT2B

Organism
Homo sapiens (Human)
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. 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.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei2585 – 25851S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2587 – 25871S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei2629 – 26291S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi2655 – 26551ZincBy similarity
Metal bindingi2703 – 27031ZincBy similarity
Binding sitei2704 – 27041S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi2705 – 27051ZincBy similarity
Metal bindingi2710 – 27101ZincBy 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 fingeri959 – 100648CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1201 – 125252PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1249 – 130355PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1335 – 139662PHD-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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-HSA-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
Trithorax homolog 2
WW domain-binding protein 7
Short name:
WBP-7
Gene namesi
Name:KMT2B
Synonyms:HRX2, KIAA0304, MLL2, MLL4, TRX2, WBP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:15840. KMT2B.

Subcellular locationi

GO - Cellular componenti

  • histone methyltransferase complex Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2189112.

Polymorphism and mutation databases

BioMutaiKMT2B.
DMDMi12643900.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 27152714Histone-lysine N-methyltransferase 2BPRO_0000124881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei113 – 1131PhosphoserineBy similarity
Modified residuei114 – 1141PhosphoserineBy similarity
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei351 – 3511PhosphoserineCombined sources
Modified residuei821 – 8211PhosphoserineCombined sources
Modified residuei844 – 8441PhosphoserineCombined sources
Modified residuei861 – 8611PhosphoserineCombined sources
Modified residuei936 – 9361PhosphoserineCombined sources
Modified residuei1032 – 10321PhosphoserineCombined sources
Modified residuei1035 – 10351PhosphoserineCombined sources
Modified residuei1092 – 10921PhosphoserineCombined sources
Modified residuei1095 – 10951PhosphoserineCombined sources
Modified residuei1930 – 19301PhosphoserineCombined sources
Modified residuei1936 – 19361PhosphoserineCombined sources
Modified residuei2068 – 20681PhosphothreonineCombined sources
Modified residuei2083 – 20831PhosphothreonineCombined sources
Modified residuei2288 – 22881PhosphoserineCombined sources
Modified residuei2348 – 23481PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9UMN6.
MaxQBiQ9UMN6.
PaxDbiQ9UMN6.
PeptideAtlasiQ9UMN6.
PRIDEiQ9UMN6.

PTM databases

iPTMnetiQ9UMN6.
PhosphoSiteiQ9UMN6.

Expressioni

Tissue specificityi

Widely expressed. Highest levels in testis. Also found in brain, bone marrow, heart, muscle, kidney, placenta, spleen, thymus, prostate, ovary, intestine, colon, peripheral blood lymphocytes and pancreas. Often amplified in pancreatic carcinomas.

Gene expression databases

CleanExiHS_MLL2.
GenevisibleiQ9UMN6. HS.

Organism-specific databases

HPAiHPA006487.

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-765774,EBI-389883
WDR5P619642EBI-765774,EBI-540834

Protein-protein interaction databases

BioGridi115104. 34 interactions.
DIPiDIP-34598N.
IntActiQ9UMN6. 32 interactions.
MINTiMINT-1187865.
STRINGi9606.ENSP00000222270.

Chemistry

BindingDBiQ9UMN6.

Structurei

Secondary structure

1
2715
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi970 – 9734Combined sources
Beta strandi979 – 9813Combined sources
Helixi982 – 9854Combined sources
Helixi988 – 9903Combined sources
Helixi1001 – 10033Combined sources
Helixi1006 – 101510Combined sources
Helixi2510 – 25123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UVMX-ray1.57B2508-2517[»]
4ERZX-ray1.75D/E/F2504-2517[»]
4PZIX-ray2.15A955-1020[»]
ProteinModelPortaliQ9UMN6.
SMRiQ9UMN6. Positions 956-1016, 1354-1393, 2541-2715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1727 – 178357FYR N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2411 – 249282FYR C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2575 – 2691117SETPROSITE-ProRule annotationAdd
BLAST
Domaini2699 – 271517Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2652 – 26532S-adenosyl-L-methionine bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi26 – 3712Poly-GlyAdd
BLAST
Compositional biasi248 – 2558Poly-Pro
Compositional biasi362 – 39837Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi402 – 771370Pro-richAdd
BLAST
Compositional biasi808 – 8125Poly-Gln
Compositional biasi1963 – 19708Poly-Pro
Compositional biasi2251 – 22599Poly-Pro

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 fingeri959 – 100648CXXC-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1201 – 125252PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1249 – 130355PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1335 – 139662PHD-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1084. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00760000119228.
HOVERGENiHBG100043.
InParanoidiQ9UMN6.
KOiK14959.
OMAiKRTGPHL.
OrthoDBiEOG091G001P.
PhylomeDBiQ9UMN6.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UMN6-1) [UniParc]FASTAAdd to basket
Also known as: Long

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
MAAAAGGGSC PGPGSARGRF PGRPRGAGGG GGRGGRGNGA ERVRVALRRG
60 70 80 90 100
GGATGPGGAE PGEDTALLRL LGLRRGLRRL RRLWAGPRVQ RGRGRGRGRG
110 120 130 140 150
WGPSRGCVPE EESSDGESDE EEFQGFHSDE DVAPSSLRSA LRSQRGRAPR
160 170 180 190 200
GRGRKHKTTP LPPPRLADVA PTPPKTPARK RGEEGTERMV QALTELLRRA
210 220 230 240 250
QAPQAPRSRA CEPSTPRRSR GRPPGRPAGP CRRKQQAVVV AEAAVTIPKP
260 270 280 290 300
EPPPPVVPVK HQTGSWKCKE GPGPGPGTPR RGGQSSRGGR GGRGRGRGGG
310 320 330 340 350
LPFVIKFVSR AKKVKMGQLS LGLESGQGQG QHEESWQDVP QRRVGSGQGG
360 370 380 390 400
SPCWKKQEQK LDDEEEEKKE EEEKDKEGEE KEERAVAEEM MPAAEKEEAK
410 420 430 440 450
LPPPPLTPPA PSPPPPLPPP STSPPPPLCP PPPPPVSPPP LPSPPPPPAQ
460 470 480 490 500
EEQEESPPPV VPATCSRKRG RPPLTPSQRA EREAARAGPE GTSPPTPTPS
510 520 530 540 550
TATGGPPEDS PTVAPKSTTF LKNIRQFIMP VVSARSSRVI KTPRRFMDED
560 570 580 590 600
PPKPPKVEVS PVLRPPITTS PPVPQEPAPV PSPPRAPTPP STPVPLPEKR
610 620 630 640 650
RSILREPTFR WTSLTRELPP PPPAPPPPPA PSPPPAPATS SRRPLLLRAP
660 670 680 690 700
QFTPSEAHLK IYESVLTPPP LGAPEAPEPE PPPADDSPAE PEPRAVGRTN
710 720 730 740 750
HLSLPRFAPV VTTPVKAEVS PHGAPALSNG PQTQAQLLQP LQALQTQLLP
760 770 780 790 800
QALPPPQPQL QPPPSPQQMP PLEKARIAGV GSLPLSGVEE KMFSLLKRAK
810 820 830 840 850
VQLFKIDQQQ QQKVAASMPL SPGGQMEEVA GAVKQISDRG PVRSEDESVE
860 870 880 890 900
AKRERPSGPE SPVQGPRIKH VCRHAAVALG QARAMVPEDV PRLSALPLRD
910 920 930 940 950
RQDLATEDTS SASETESVPS RSRRGKVEAA GPGGESEPTG SGGTLAHTPR
960 970 980 990 1000
RSLPSHHGKK MRMARCGHCR GCLRVQDCGS CVNCLDKPKF GGPNTKKQCC
1010 1020 1030 1040 1050
VYRKCDKIEA RKMERLAKKG RTIVKTLLPW DSDESPEASP GPPGPRRGAG
1060 1070 1080 1090 1100
AGGPREEVVA HPGPEEQDSL LQRKSARRCV KQRPSYDIFE DSDDSEPGGP
1110 1120 1130 1140 1150
PAPRRRTPRE NELPLPEPEE QSRPRKPTLQ PVLQLKARRR LDKDALAPGP
1160 1170 1180 1190 1200
FASFPNGWTG KQKSPDGVHR VRVDFKEDCD LENVWLMGGL SVLTSVPGGP
1210 1220 1230 1240 1250
PMVCLLCASK GLHELVFCQV CCDPFHPFCL EEAERPLPQH HDTWCCRRCK
1260 1270 1280 1290 1300
FCHVCGRKGR GSKHLLECER CRHAYHPACL GPSYPTRATR KRRHWICSAC
1310 1320 1330 1340 1350
VRCKSCGATP GKNWDVEWSG DYSLCPRCTQ LYEKGNYCPI CTRCYEDNDY
1360 1370 1380 1390 1400
ESKMMQCAQC DHWVHAKCEG LSDEDYEILS GLPDSVLYTC GPCAGAAQPR
1410 1420 1430 1440 1450
WREALSGALQ GGLRQVLQGL LSSKVVGPLL LCTQCGPDGK QLHPGPCGLQ
1460 1470 1480 1490 1500
AVSQRFEDGH YKSVHSFMED MVGILMRHSE EGETPDRRAG GQMKGLLLKL
1510 1520 1530 1540 1550
LESAFGWFDA HDPKYWRRST RLPNGVLPNA VLPPSLDHVY AQWRQQEPET
1560 1570 1580 1590 1600
PESGQPPGDP SAAFQGKDPA AFSHLEDPRQ CALCLKYGDA DSKEAGRLLY
1610 1620 1630 1640 1650
IGQNEWTHVN CAIWSAEVFE ENDGSLKNVH AAVARGRQMR CELCLKPGAT
1660 1670 1680 1690 1700
VGCCLSSCLS NFHFMCARAS YCIFQDDKKV FCQKHTDLLD GKEIVNPDGF
1710 1720 1730 1740 1750
DVLRRVYVDF EGINFKRKFL TGLEPDAINV LIGSIRIDSL GTLSDLSDCE
1760 1770 1780 1790 1800
GRLFPIGYQC SRLYWSTVDA RRRCWYRCRI LEYRPWGPRE EPAHLEAAEE
1810 1820 1830 1840 1850
NQTIVHSPAP SSEPPGGEDP PLDTDVLVPG APERHSPIQN LDPPLRPDSG
1860 1870 1880 1890 1900
SAPPPAPRSF SGARIKVPNY SPSRRPLGGV SFGPLPSPGS PSSLTHHIPT
1910 1920 1930 1940 1950
VGDPDFPAPP RRSRRPSPLA PRPPPSRWAS PPLKTSPQLR VPPPTSVVTA
1960 1970 1980 1990 2000
LTPTSGELAP PGPAPSPPPP EDLGPDFEDM EVVSGLSAAD LDFAASLLGT
2010 2020 2030 2040 2050
EPFQEEIVAA GAMGSSHGGP GDSSEEESSP TSRYIHFPVT VVSAPGLAPS
2060 2070 2080 2090 2100
ATPGAPRIEQ LDGVDDGTDS EAEAVQQPRG QGTPPSGPGV VRAGVLGAAG
2110 2120 2130 2140 2150
DRARPPEDLP SEIVDFVLKN LGGPGDGGAG PREESLPPAP PLANGSQPSQ
2160 2170 2180 2190 2200
GLTASPADPT RTFAWLPGAP GVRVLSLGPA PEPPKPATSK IILVNKLGQV
2210 2220 2230 2240 2250
FVKMAGEGEP VPPPVKQPPL PPTISPTAPT SWTLPPGPLL GVLPVVGVVR
2260 2270 2280 2290 2300
PAPPPPPPPL TLVLSSGPAS PPRQAIRVKR VSTFSGRSPP APPPYKAPRL
2310 2320 2330 2340 2350
DEDGEASEDT PQVPGLGSGG FSRVRMKTPT VRGVLDLDRP GEPAGEESPG
2360 2370 2380 2390 2400
PLQERSPLLP LPEDGPPQVP DGPPDLLLES QWHHYSGEAS SSEEEPPSPD
2410 2420 2430 2440 2450
DKENQAPKRT GPHLRFEISS EDGFSVEAES LEGAWRTLIE KVQEARGHAR
2460 2470 2480 2490 2500
LRHLSFSGMS GARLLGIHHD AVIFLAEQLP GAQRCQHYKF RYHQQGEGQE
2510 2520 2530 2540 2550
EPPLNPHGAA RAEVYLRKCT FDMFNFLASQ HRVLPEGATC DEEEDEVQLR
2560 2570 2580 2590 2600
STRRATSLEL PMAMRFRHLK KTSKEAVGVY RSAIHGRGLF CKRNIDAGEM
2610 2620 2630 2640 2650
VIEYSGIVIR SVLTDKREKF YDGKGIGCYM FRMDDFDVVD ATMHGNAARF
2660 2670 2680 2690 2700
INHSCEPNCF SRVIHVEGQK HIVIFALRRI LRGEELTYDY KFPIEDASNK
2710
LPCNCGAKRC RRFLN
Length:2,715
Mass (Da):293,515
Last modified:May 1, 2000 - v1
Checksum:iC0615B981BBEB7BF
GO
Isoform 2 (identifier: Q9UMN6-2) [UniParc]FASTAAdd to basket
Also known as: Truncated

The sequence of this isoform differs from the canonical sequence as follows:
     532-582: VSARSSRVIK...VPQEPAPVPS → PLSQSLLLPM...PRCPLTGLQL
     583-2715: Missing.

Show »
Length:582
Mass (Da):61,562
Checksum:i8B2EE4B04969CF76
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti834 – 8341K → E in AAD17932 (PubMed:10409430).Curated
Sequence conflicti941 – 9411S → Y in AAD17932 (PubMed:10409430).Curated
Sequence conflicti1317 – 13171E → Q in AAD17932 (PubMed:10409430).Curated
Sequence conflicti1362 – 13621H → Y in AAD17932 (PubMed:10409430).Curated
Sequence conflicti1438 – 14381D → N in AAD17932 (PubMed:10409430).Curated
Sequence conflicti1918 – 19203PLA → GTR in AAH09337 (PubMed:15489334).Curated
Sequence conflicti2622 – 26221D → H in AAD26112 (PubMed:10409430).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti172 – 1721T → I.
Corresponds to variant rs60207923 [ dbSNP | Ensembl ].
VAR_061913
Natural varianti587 – 5871P → R.
Corresponds to variant rs2242519 [ dbSNP | Ensembl ].
VAR_046563
Natural varianti754 – 7541P → L.
Corresponds to variant rs179686 [ dbSNP | Ensembl ].
VAR_046564
Natural varianti1097 – 10971P → L.
Corresponds to variant rs34014681 [ dbSNP | Ensembl ].
VAR_046565
Natural varianti1829 – 18291P → L.
Corresponds to variant rs16970649 [ dbSNP | Ensembl ].
VAR_052653
Natural varianti2364 – 23641D → G.
Corresponds to variant rs231591 [ dbSNP | Ensembl ].
VAR_052654
Natural varianti2408 – 24081K → N.
Corresponds to variant rs36062432 [ dbSNP | Ensembl ].
VAR_052655

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei532 – 58251VSARS…APVPS → PLSQSLLLPMTLQLSLSLGQ WAAPTTSACLDSPLWSPLLL RPRCPLTGLQL in isoform 2. CuratedVSP_006668Add
BLAST
Alternative sequencei583 – 27152133Missing in isoform 2. CuratedVSP_006669Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007041 mRNA. Translation: CAB45385.1.
AD000671 Genomic DNA. No translation available.
AF186605 mRNA. Translation: AAD56420.1.
AB002302 mRNA. Translation: BAA20763.3.
BC009337 mRNA. Translation: AAH09337.2.
BC007353 mRNA. Translation: AAH07353.3.
AF104918 mRNA. Translation: AAD17932.1.
AF105279 mRNA. Translation: AAD26113.1.
AF105280 mRNA. Translation: AAD26112.1.
CCDSiCCDS46055.1. [Q9UMN6-1]
RefSeqiNP_055542.1. NM_014727.2. [Q9UMN6-1]
UniGeneiHs.676457.
Hs.92236.

Genome annotation databases

EnsembliENST00000420124; ENSP00000398837; ENSG00000272333. [Q9UMN6-1]
GeneIDi9757.
KEGGihsa:9757.
UCSCiuc021usv.1. human. [Q9UMN6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007041 mRNA. Translation: CAB45385.1.
AD000671 Genomic DNA. No translation available.
AF186605 mRNA. Translation: AAD56420.1.
AB002302 mRNA. Translation: BAA20763.3.
BC009337 mRNA. Translation: AAH09337.2.
BC007353 mRNA. Translation: AAH07353.3.
AF104918 mRNA. Translation: AAD17932.1.
AF105279 mRNA. Translation: AAD26113.1.
AF105280 mRNA. Translation: AAD26112.1.
CCDSiCCDS46055.1. [Q9UMN6-1]
RefSeqiNP_055542.1. NM_014727.2. [Q9UMN6-1]
UniGeneiHs.676457.
Hs.92236.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UVMX-ray1.57B2508-2517[»]
4ERZX-ray1.75D/E/F2504-2517[»]
4PZIX-ray2.15A955-1020[»]
ProteinModelPortaliQ9UMN6.
SMRiQ9UMN6. Positions 956-1016, 1354-1393, 2541-2715.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115104. 34 interactions.
DIPiDIP-34598N.
IntActiQ9UMN6. 32 interactions.
MINTiMINT-1187865.
STRINGi9606.ENSP00000222270.

Chemistry

BindingDBiQ9UMN6.
ChEMBLiCHEMBL2189112.

PTM databases

iPTMnetiQ9UMN6.
PhosphoSiteiQ9UMN6.

Polymorphism and mutation databases

BioMutaiKMT2B.
DMDMi12643900.

Proteomic databases

EPDiQ9UMN6.
MaxQBiQ9UMN6.
PaxDbiQ9UMN6.
PeptideAtlasiQ9UMN6.
PRIDEiQ9UMN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000420124; ENSP00000398837; ENSG00000272333. [Q9UMN6-1]
GeneIDi9757.
KEGGihsa:9757.
UCSCiuc021usv.1. human. [Q9UMN6-1]

Organism-specific databases

CTDi9757.
GeneCardsiKMT2B.
HGNCiHGNC:15840. KMT2B.
HPAiHPA006487.
MIMi606834. gene.
neXtProtiNX_Q9UMN6.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1084. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00760000119228.
HOVERGENiHBG100043.
InParanoidiQ9UMN6.
KOiK14959.
OMAiKRTGPHL.
OrthoDBiEOG091G001P.
PhylomeDBiQ9UMN6.

Enzyme and pathway databases

ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.

Miscellaneous databases

GeneWikiiMLL4.
GenomeRNAii9757.
PROiQ9UMN6.
SOURCEiSearch...

Gene expression databases

CleanExiHS_MLL2.
GenevisibleiQ9UMN6. HS.

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...

Entry informationi

Entry nameiKMT2B_HUMAN
AccessioniPrimary (citable) accession number: Q9UMN6
Secondary accession number(s): O15022
, O95836, Q96GP2, Q96IP3, Q9UK25, Q9Y668, Q9Y669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 175 of the entry and version 1 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

Caution

This protein was first named MLL2 by PubMed:10637508 and PubMed:10409430. MLL2 corresponds to another protein located on chromosome 12 (see AC O14686). 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 19
    Human chromosome 19: 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

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.