Q8NEZ4 (MLL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 106.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Histone-lysine N-methyltransferase MLL3 EC=2.1.1.43 Alternative name(s): Homologous to ALR protein Lysine N-methyltransferase 2C Short name=KMT2C Myeloid/lymphoid or mixed-lineage leukemia protein 3 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 4911 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Central component of the MLL2/MLL3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. MLL3 may be a catalytic subunit of this complex. May be involved in leukemogenesis and developmental disorder. Ref.16 |
| Catalytic activity | S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.16 |
| Subunit structure | Component of the MLL2/MLL3 complex (also named ASCOM complex), at least composed of MLL2, MLL3, ASH2L, RBBP5, DPY30, NCOA6, WDR5, MEN1, KDM6A and PAXIP1/PTIP. Component of the MLL3/MLL4 complex at least composed of MLL3, MLL4, ASH2L, RBBP5, DPY30, WDR5, NCOA6, KDM6A, PAXIP1/PTIP and C16orf53/PA1. Interacts with histone H3. Ref.8 |
| Subcellular location | Nucleus Probable. |
| Tissue specificity | Highly expressed in testis and ovary, followed by brain and liver. Also expressed in placenta, peripherical blood, fetal thymus, heart, lung and kidney. Within brain, expression was highest in hippocampus, caudate nucleus, and substantia nigra. Not detected in skeletal muscle and fetal liver. |
| Domain | The SET domain interacts with histone H3 but not H2A, H2B and H4, and may have a H3 lysine specific methylation activity. |
| Miscellaneous | Found in a critical region of chromosome 7, which is commonly deleted in malignant myeloid disorders. Partial duplication of the MLL3 gene are found in the juxtacentromeric region of chromosomes 1, 2, 13 and 21. Juxtacentromeric reshuffling of the MLL3 gene has generated the BAGE genes. |
| Sequence similarities | Belongs to the histone-lysine methyltransferase family. TRX/MLL subfamily. Contains 1 A.T hook DNA-binding domain. Contains 1 DHHC-type zinc finger. Contains 1 FYR C-terminal domain. Contains 1 FYR N-terminal domain. Contains 6 PHD-type zinc fingers. Contains 1 post-SET domain. Contains 1 RING-type zinc finger. Contains 1 SET domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Coiled coil Repeat Zinc-finger |
| Ligand | DNA-binding Metal-binding S-adenosyl-L-methionine Zinc |
| Molecular function | Activator Chromatin regulator Methyltransferase Transferase |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | intracellular signal transduction Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| NCOA6 | Q14686 | 4 | EBI-1042997,EBI-78670 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q8NEZ4-1) 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. | ||||||
| Isoform 2 (identifier: Q8NEZ4-2) The sequence of this isoform differs from the canonical sequence as follows: 1-939: Missing. 3890-3890: Q → QVRQLSLLPLMEPIIGVNFAHFLPYGSGQFNSGNRLLGTFGSATLEGVSDYYSQLIYK 4721-4724: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 3 (identifier: Q8NEZ4-3) The sequence of this isoform differs from the canonical sequence as follows: 3890-3890: Q → QVRQLSLLPLMEPIIGVNFAHFLPYGSGQFNSGNRLLGTFGSATLEGVSDYYSQLIYK | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 4911 | 4911 | Histone-lysine N-methyltransferase MLL3 | PRO_0000124879 | ||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||
| Domain | 4545 – 4605 | 61 | FYR N-terminal | |||||||||||||||||||||||||||||||
| Domain | 4606 – 4691 | 86 | FYR C-terminal | |||||||||||||||||||||||||||||||
| Domain | 4770 – 4891 | 122 | SET | |||||||||||||||||||||||||||||||
| Domain | 4895 – 4911 | 17 | Post-SET | |||||||||||||||||||||||||||||||
| DNA binding | 34 – 46 | 13 | A.T hook | |||||||||||||||||||||||||||||||
| Zinc finger | 341 – 391 | 51 | PHD-type 1 | |||||||||||||||||||||||||||||||
| Zinc finger | 344 – 389 | 46 | RING-type | |||||||||||||||||||||||||||||||
| Zinc finger | 388 – 438 | 51 | PHD-type 2 | |||||||||||||||||||||||||||||||
| Zinc finger | 436 – 489 | 54 | DHHC-type | |||||||||||||||||||||||||||||||
| Zinc finger | 464 – 520 | 57 | PHD-type 3 | |||||||||||||||||||||||||||||||
| Zinc finger | 957 – 1010 | 54 | PHD-type 4 | |||||||||||||||||||||||||||||||
| Zinc finger | 1007 – 1057 | 51 | PHD-type 5 | |||||||||||||||||||||||||||||||
| Zinc finger | 1084 – 1139 | 56 | PHD-type 6 | |||||||||||||||||||||||||||||||
| Region | 4848 – 4849 | 2 | S-adenosyl-L-methionine binding By similarity | |||||||||||||||||||||||||||||||
| Coiled coil | 92 – 112 | 21 | Potential | |||||||||||||||||||||||||||||||
| Coiled coil | 644 – 672 | 29 | Potential | |||||||||||||||||||||||||||||||
| Coiled coil | 1338 – 1366 | 29 | Potential | |||||||||||||||||||||||||||||||
| Coiled coil | 1754 – 1787 | 34 | Potential | |||||||||||||||||||||||||||||||
| Coiled coil | 3054 – 3081 | 28 | Potential | |||||||||||||||||||||||||||||||
| Coiled coil | 3173 – 3272 | 100 | Potential | |||||||||||||||||||||||||||||||
| Coiled coil | 3391 – 3433 | 43 | Potential | |||||||||||||||||||||||||||||||
| Compositional bias | 1719 – 1796 | 78 | Gln-rich | |||||||||||||||||||||||||||||||
| Compositional bias | 1834 – 2281 | 448 | Pro-rich | |||||||||||||||||||||||||||||||
| Compositional bias | 2412 – 2630 | 219 | Pro-rich | |||||||||||||||||||||||||||||||
| Compositional bias | 2690 – 2786 | 97 | Asp-rich | |||||||||||||||||||||||||||||||
| Compositional bias | 3012 – 3509 | 498 | Gln-rich | |||||||||||||||||||||||||||||||
| Compositional bias | 3277 – 3381 | 105 | Pro-rich | |||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||
| Metal binding | 4851 | 1 | Zinc By similarity | |||||||||||||||||||||||||||||||
| Metal binding | 4899 | 1 | Zinc By similarity | |||||||||||||||||||||||||||||||
| Metal binding | 4901 | 1 | Zinc By similarity | |||||||||||||||||||||||||||||||
| Metal binding | 4906 | 1 | Zinc By similarity | |||||||||||||||||||||||||||||||
| Binding site | 4825 | 1 | S-adenosyl-L-methionine By similarity | |||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||
| Modified residue | 758 | 1 | N6-acetyllysine Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 827 | 1 | N6-acetyllysine Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 1508 | 1 | N6-acetyllysine Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 1772 | 1 | N6-acetyllysine Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 2009 | 1 | N6-acetyllysine Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 2802 | 1 | N6-acetyllysine Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 2809 | 1 | N6-acetyllysine Ref.10 Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 2832 | 1 | N6-acetyllysine Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 3714 | 1 | N6-acetyllysine Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 3945 | 1 | N6-acetyllysine Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 4018 | 1 | Phosphotyrosine Ref.9 | |||||||||||||||||||||||||||||||
| Modified residue | 4022 | 1 | Phosphoserine Ref.9 | |||||||||||||||||||||||||||||||
| Modified residue | 4034 | 1 | Phosphoserine Ref.11 | |||||||||||||||||||||||||||||||
| Modified residue | 4050 | 1 | Phosphoserine Ref.11 | |||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 939 | 939 | Missing in isoform 2. | VSP_008561 | ||||||||||||||||||||||||||||||
| Alternative sequence | 3890 | 1 | Q → QVRQLSLLPLMEPIIGVNFA HFLPYGSGQFNSGNRLLGTF GSATLEGVSDYYSQLIYK in isoform 2 and isoform 3. | VSP_008562 | ||||||||||||||||||||||||||||||
| Alternative sequence | 4721 – 4724 | 4 | Missing in isoform 2. | VSP_036223 | ||||||||||||||||||||||||||||||
| Natural variant | 291 | 1 | L → F. Corresponds to variant rs56850341 [ dbSNP | Ensembl ]. | VAR_061911 | ||||||||||||||||||||||||||||||
| Natural variant | 316 | 1 | T → S. Corresponds to variant rs10454320 [ dbSNP | Ensembl ]. | VAR_061912 | ||||||||||||||||||||||||||||||
| Natural variant | 347 | 1 | C → G in a colorectal cancer sample; somatic mutation. Ref.15 | VAR_036311 | ||||||||||||||||||||||||||||||
| Natural variant | 400 | 1 | D → N in a colorectal cancer sample; somatic mutation. Ref.15 | VAR_036312 | ||||||||||||||||||||||||||||||
| Natural variant | 478 | 1 | L → W in a colorectal cancer sample; somatic mutation. Ref.15 | VAR_036313 | ||||||||||||||||||||||||||||||
| Natural variant | 526 | 1 | R → P. Ref.1 Corresponds to variant rs3735156 [ dbSNP | Ensembl ]. | VAR_057360 | ||||||||||||||||||||||||||||||
| Natural variant | 823 | 1 | I → N. Corresponds to variant rs2838171 [ dbSNP | Ensembl ]. | VAR_017118 | ||||||||||||||||||||||||||||||
| Natural variant | 823 | 1 | I → T. Corresponds to variant rs2838171 [ dbSNP | Ensembl ]. | VAR_017117 | ||||||||||||||||||||||||||||||
| Natural variant | 1836 | 1 | S → N. Corresponds to variant rs11771635 [ dbSNP | Ensembl ]. | VAR_057361 | ||||||||||||||||||||||||||||||
| Natural variant | 2008 | 1 | T → A. Corresponds to variant rs6951159 [ dbSNP | Ensembl ]. | VAR_057362 | ||||||||||||||||||||||||||||||
| Natural variant | 2412 | 1 | P → T. Corresponds to variant rs13231116 [ dbSNP | Ensembl ]. | VAR_057363 | ||||||||||||||||||||||||||||||
| Natural variant | 2600 | 1 | P → A. Corresponds to variant rs2270234 [ dbSNP | Ensembl ]. | VAR_057364 | ||||||||||||||||||||||||||||||
| Natural variant | 3698 | 1 | T → S in a colorectal cancer sample; somatic mutation. Ref.15 | VAR_036314 | ||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 579 | 1 | A → T in AAK00583. Ref.1 | |||||||||||||||||||||||||||||||
| Sequence conflict | 1286 | 1 | M → V in AAK00583. Ref.1 | |||||||||||||||||||||||||||||||
| Sequence conflict | 2360 | 1 | P → S in AAK00583. Ref.1 | |||||||||||||||||||||||||||||||
| Sequence conflict | 2797 | 1 | K → R in AAK00583. Ref.1 | |||||||||||||||||||||||||||||||
| Sequence conflict | 2882 | 1 | T → A in AAK00583. Ref.1 | |||||||||||||||||||||||||||||||
| Sequence conflict | 3289 | 1 | P → S in BAC11409. Ref.6 | |||||||||||||||||||||||||||||||
| Sequence conflict | 3428 | 1 | R → W in BAC11409. Ref.6 | |||||||||||||||||||||||||||||||
| Sequence conflict | 4613 | 1 | I → V in AK022687. Ref.6 | |||||||||||||||||||||||||||||||
| Sequence conflict | 4866 | 1 | H → P in AK022687. Ref.6 | |||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||
| Turn | 345 – 347 | 3 | ||||||||||||||||||||||||||||||||
| Turn | 353 – 355 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 356 – 358 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 360 – 362 | 3 | ||||||||||||||||||||||||||||||||
| Turn | 368 – 372 | 5 | ||||||||||||||||||||||||||||||||
| Turn | 377 – 379 | 3 | ||||||||||||||||||||||||||||||||
| Turn | 386 – 388 | 3 | ||||||||||||||||||||||||||||||||
| Turn | 392 – 394 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 403 – 405 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 407 – 409 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 412 – 414 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 415 – 417 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 418 – 420 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 433 – 436 | 4 | ||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "MLL3, a new human member of the TRX/MLL gene family, maps to 7q36, a chromosome region frequently deleted in myeloid leukaemia." Ruault M., Brun M.-E., Ventura M., Roizes G., De Sario A. Gene 284:73-81(2002) [PubMed: 11891048] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-526. Tissue: Fetal thymus. |
| [2] | "Novel human HALR (MLL3) gene encodes a protein homologous to ALR and to ALL-1 involved in leukemia, and maps to chromosome 7q36 associated with leukemia and developmental defects." Tan Y.C., Chow V.T. Cancer Detect. Prev. 25:454-469(2001) [PubMed: 11718452] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Cervix carcinoma. |
| [3] | "The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. Wilson R.K.Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:143-150(2000) [PubMed: 10819331] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 556-3865 (ISOFORM 1). Tissue: Brain. |
| [5] | "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION. |
| [6] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3193-3865 AND 4460-4911. Tissue: Placenta. |
| [7] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Testis. |
| [8] | "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: 12482968] [Abstract] Cited for: INTERACTION WITH MLL2/MLL3 COMPLEX (ISOFORM 2). Tissue: Cervix carcinoma. |
| [9] | "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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4018 AND SER-4022, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [10] | "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2809, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [11] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4034 AND SER-4050, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-758; LYS-827; LYS-1508; LYS-1772; LYS-2009; LYS-2802; LYS-2809; LYS-2832; LYS-3714 AND LYS-3945, MASS SPECTROMETRY. |
| [13] | "Solution structure of the first and second PHD domain from myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 342-439. |
| [14] | "Solution structure of the HMG box of human myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog." RIKEN structural genomics initiative (RSGI) Submitted (APR-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1624-1713. |
| [15] | "The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E.Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-347; ASN-400; TRP-478 AND SER-3698. |
| [16] | "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: 17500065] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL3/MLL4 COMPLEX. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AY024361 mRNA. Translation: AAK00583.1. AF264750 mRNA. Translation: AAF74766.2. AC006017 Genomic DNA. Translation: AAD45822.1. AC104692 Genomic DNA. No translation available. AC005631 Genomic DNA. No translation available. AB040939 mRNA. Translation: BAA96030.2. AK022687 mRNA. No translation available. AK075113 mRNA. Translation: BAC11409.1. AL833924 mRNA. Translation: CAD38780.1. | ||||||||||||||||||
| IPI | IPI00168806. IPI00375729. IPI00916332. | ||||||||||||||||||
| RefSeq | NP_733751.2. NM_170606.2. | ||||||||||||||||||
| UniGene | Hs.647120. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | Q8NEZ4. | ||||||||||||||||||
| SMR | Q8NEZ4. Positions 282-520, 956-1138, 1624-1713, 4542-4691, 4756-4911. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-48649N. | ||||||||||||||||||
| IntAct | Q8NEZ4. 9 interactions. | ||||||||||||||||||
| STRING | Q8NEZ4. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | Q8NEZ4. | ||||||||||||||||||
Polymorphism databases | |||||||||||||||||||
| DMDM | 221222521. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | Q8NEZ4. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000262189; ENSP00000262189; ENSG00000055609. | ||||||||||||||||||
| GeneID | 58508. | ||||||||||||||||||
| KEGG | hsa:58508. | ||||||||||||||||||
| UCSC | uc003wla.1. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 58508. | ||||||||||||||||||
| GeneCards | GC07M151832. | ||||||||||||||||||
| H-InvDB | HIX0007238. | ||||||||||||||||||
| HGNC | HGNC:13726. MLL3. | ||||||||||||||||||
| MIM | 606833. gene. | ||||||||||||||||||
| neXtProt | NX_Q8NEZ4. | ||||||||||||||||||
| PharmGKB | PA30847. | ||||||||||||||||||
| HUGE | Search... | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| GeneTree | ENSGT00580000081416. | ||||||||||||||||||
| HOVERGEN | HBG045586. | ||||||||||||||||||
| InParanoid | Q8NEZ4. | ||||||||||||||||||
| OMA | DTSRQNK. | ||||||||||||||||||
| PhylomeDB | Q8NEZ4. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | Q8NEZ4. | ||||||||||||||||||
| Bgee | Q8NEZ4. | ||||||||||||||||||
| CleanEx | HS_MLL3. | ||||||||||||||||||
| Genevestigator | Q8NEZ4. | ||||||||||||||||||
| GermOnline | ENSG00000055609. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR017956. AT_hook_DNA-bd_motif. IPR003889. FYrich_C. IPR018516. FYrich_C_subgr. IPR003888. FYrich_N. IPR018518. FYrich_N_subgr. IPR000910. HMG_HMG1/HMG2. IPR000637. HMGI/Y_DNA-bd_CS. IPR003616. Post-SET_dom. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR001214. SET_dom. IPR001594. Znf_DHHC_palmitoyltrfase. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 6 hits. | ||||||||||||||||||
| KO | K09188. | ||||||||||||||||||
| Pfam | PF05965. FYRC. 1 hit. PF05964. FYRN. 1 hit. PF00628. PHD. 2 hits. PF00856. SET. 1 hit. [Graphical view] | ||||||||||||||||||
| SMART | SM00384. AT_hook. 2 hits. SM00109. C1. 2 hits. SM00542. FYRC. 1 hit. SM00541. FYRN. 1 hit. SM00398. HMG. 1 hit. SM00249. PHD. 8 hits. SM00508. PostSET. 1 hit. SM00184. RING. 4 hits. SM00317. SET. 1 hit. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF57903. FYVE_PHD_ZnF. 6 hits. | ||||||||||||||||||
| PROSITE | PS51543. FYRC. 1 hit. PS51542. FYRN. 1 hit. PS00354. HMGI_Y. 1 hit. PS50868. POST_SET. 1 hit. PS50280. SET. 1 hit. PS50216. ZF_DHHC. 1 hit. PS01359. ZF_PHD_1. 5 hits. PS50016. ZF_PHD_2. 6 hits. PS50089. ZF_RING_2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| NextBio | 65023. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | MLL3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8NEZ4 Secondary accession number(s): Q8NC02 Q9UDR7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 7 Human chromosome 7: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with