Details for: KMT2A

Gene ID: 4297

Symbol: KMT2A

Ensembl ID: ENSG00000118058

Description: lysine methyltransferase 2A

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: polychromatophilic erythroblast (CL0000550)
    Fold Change: 512.8412
    Cell Significance Index: -79.7700
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 297.7014
    Cell Significance Index: -75.5100
  • Cell Name: embryonic stem cell (CL0002322)
    Fold Change: 182.0863
    Cell Significance Index: -75.0100
  • Cell Name: smooth muscle fiber of ileum (CL1000278)
    Fold Change: 178.6612
    Cell Significance Index: -84.3500
  • Cell Name: mucosal type mast cell (CL0000485)
    Fold Change: 167.3817
    Cell Significance Index: -68.0000
  • Cell Name: peripheral blood mononuclear cell (CL2000001)
    Fold Change: 151.5304
    Cell Significance Index: -77.9500
  • Cell Name: ciliated cell of the bronchus (CL0002332)
    Fold Change: 71.5323
    Cell Significance Index: -68.3000
  • Cell Name: orthochromatic erythroblast (CL0000552)
    Fold Change: 67.4477
    Cell Significance Index: -83.1600
  • Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
    Fold Change: 29.3184
    Cell Significance Index: -78.5400
  • Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
    Fold Change: 26.4272
    Cell Significance Index: -81.1700
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 21.4303
    Cell Significance Index: -84.5700
  • Cell Name: epidermal Langerhans cell (CL0002457)
    Fold Change: 20.8079
    Cell Significance Index: -45.5400
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: 3.9704
    Cell Significance Index: 222.8000
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 3.2567
    Cell Significance Index: 653.3000
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 3.1558
    Cell Significance Index: 1131.9400
  • Cell Name: cortical interneuron (CL0008031)
    Fold Change: 2.6373
    Cell Significance Index: 63.2500
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: 2.5537
    Cell Significance Index: 156.9600
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 2.1666
    Cell Significance Index: 112.8600
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 1.7660
    Cell Significance Index: 350.4600
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: 1.7630
    Cell Significance Index: 77.9800
  • Cell Name: direct pathway medium spiny neuron (CL4023026)
    Fold Change: 1.6259
    Cell Significance Index: 61.5700
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 1.5385
    Cell Significance Index: 277.3400
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 1.4826
    Cell Significance Index: 42.5000
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: 1.4727
    Cell Significance Index: 181.0800
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: 1.4219
    Cell Significance Index: 19.4000
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 1.4028
    Cell Significance Index: 192.6400
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 1.2415
    Cell Significance Index: 135.0400
  • Cell Name: Purkinje cell (CL0000121)
    Fold Change: 1.1235
    Cell Significance Index: 24.6000
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 0.9410
    Cell Significance Index: 72.2100
  • Cell Name: preadipocyte (CL0002334)
    Fold Change: 0.9379
    Cell Significance Index: 18.3100
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.8961
    Cell Significance Index: 809.0900
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: 0.8329
    Cell Significance Index: 53.7400
  • Cell Name: cone retinal bipolar cell (CL0000752)
    Fold Change: 0.7765
    Cell Significance Index: 5.9900
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 0.6982
    Cell Significance Index: 381.3200
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: 0.6863
    Cell Significance Index: 303.4500
  • Cell Name: retinal rod cell (CL0000604)
    Fold Change: 0.6417
    Cell Significance Index: 7.6500
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: 0.5902
    Cell Significance Index: 37.2000
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: 0.5636
    Cell Significance Index: 26.4900
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 0.5010
    Cell Significance Index: 34.6500
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 0.4930
    Cell Significance Index: 13.4200
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 0.4729
    Cell Significance Index: 55.7800
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: 0.3794
    Cell Significance Index: 10.9300
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: 0.3467
    Cell Significance Index: 23.3100
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 0.2973
    Cell Significance Index: 38.1200
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: 0.2848
    Cell Significance Index: 7.9600
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 0.2796
    Cell Significance Index: 12.6800
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: 0.2302
    Cell Significance Index: 433.4800
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: 0.2211
    Cell Significance Index: 4.7900
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.1983
    Cell Significance Index: 37.7400
  • Cell Name: cerebellar granule cell (CL0001031)
    Fold Change: 0.1955
    Cell Significance Index: 3.3500
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: 0.1012
    Cell Significance Index: 186.6900
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: 0.0903
    Cell Significance Index: 138.9700
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 0.0676
    Cell Significance Index: 3.1500
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 0.0665
    Cell Significance Index: 42.2600
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: 0.0425
    Cell Significance Index: 1.5000
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.0177
    Cell Significance Index: 2.8800
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: 0.0153
    Cell Significance Index: 2.6100
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: 0.0108
    Cell Significance Index: 14.6300
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: -0.0025
    Cell Significance Index: -1.8100
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: -0.0202
    Cell Significance Index: -1.0600
  • Cell Name: lactocyte (CL0002325)
    Fold Change: -0.0230
    Cell Significance Index: -2.9800
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0307
    Cell Significance Index: -13.9200
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0808
    Cell Significance Index: -59.8900
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: -0.0841
    Cell Significance Index: -63.6700
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: -0.0978
    Cell Significance Index: -9.6700
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: -0.1123
    Cell Significance Index: -7.9400
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.1342
    Cell Significance Index: -75.6600
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.1386
    Cell Significance Index: -86.5400
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: -0.2010
    Cell Significance Index: -20.5300
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: -0.2111
    Cell Significance Index: -15.7300
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.2371
    Cell Significance Index: -34.4700
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.3327
    Cell Significance Index: -38.7700
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: -0.3933
    Cell Significance Index: -20.4300
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.4029
    Cell Significance Index: -84.8700
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.4167
    Cell Significance Index: -47.7400
  • Cell Name: peg cell (CL4033014)
    Fold Change: -0.4813
    Cell Significance Index: -11.1200
  • Cell Name: glutamatergic neuron (CL0000679)
    Fold Change: -0.6122
    Cell Significance Index: -6.6700
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.6469
    Cell Significance Index: -67.3600
  • Cell Name: leptomeningeal cell (CL0000708)
    Fold Change: -0.7039
    Cell Significance Index: -15.0500
  • Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
    Fold Change: -0.7377
    Cell Significance Index: -15.7100
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: -0.8581
    Cell Significance Index: -21.4500
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -0.8736
    Cell Significance Index: -69.1900
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: -0.8972
    Cell Significance Index: -15.0200
  • Cell Name: hippocampal pyramidal neuron (CL1001571)
    Fold Change: -0.9924
    Cell Significance Index: -28.3200
  • Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
    Fold Change: -0.9945
    Cell Significance Index: -34.5600
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: -1.0225
    Cell Significance Index: -32.7500
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: -1.1363
    Cell Significance Index: -30.3400
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: -1.1457
    Cell Significance Index: -70.2400
  • Cell Name: gut absorptive cell (CL0000677)
    Fold Change: -1.2165
    Cell Significance Index: -73.0300
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: -1.3286
    Cell Significance Index: -34.9400
  • Cell Name: sst GABAergic cortical interneuron (CL4023017)
    Fold Change: -1.3574
    Cell Significance Index: -26.8400
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: -1.3589
    Cell Significance Index: -44.4900
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: -1.4147
    Cell Significance Index: -45.0600
  • Cell Name: basal cell of epidermis (CL0002187)
    Fold Change: -1.4242
    Cell Significance Index: -21.6300
  • Cell Name: VIP GABAergic cortical interneuron (CL4023016)
    Fold Change: -1.4417
    Cell Significance Index: -28.9500
  • Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
    Fold Change: -1.4540
    Cell Significance Index: -30.8600
  • Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
    Fold Change: -1.4594
    Cell Significance Index: -42.8600
  • Cell Name: astrocyte of the cerebral cortex (CL0002605)
    Fold Change: -1.5115
    Cell Significance Index: -26.1400
  • Cell Name: cardiac endothelial cell (CL0010008)
    Fold Change: -1.6033
    Cell Significance Index: -23.0600
  • Cell Name: cardiac muscle cell (CL0000746)
    Fold Change: -1.6175
    Cell Significance Index: -23.8800

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** 1. **Histone methyltransferase activity**: KMT2A is a member of the SET domain family, which is characterized by its histone methyltransferase activity. 2. **Methylates H3K4**: KMT2A specifically methylates histone H3 at lysine 4 (H3K4), which is a key epigenetic mark associated with active transcription. 3. **Regulates chromatin structure**: KMT2A's methyltransferase activity influences chromatin structure, promoting the formation of open chromatin and facilitating gene expression. 4. **Interacts with other proteins**: KMT2A forms complexes with other proteins, such as WDR5, to regulate histone modification and gene expression. **Pathways and Functions:** KMT2A is involved in various cellular processes, including: 1. **Developmental biology**: KMT2A regulates the expression of genes involved in embryonic development, including hematopoiesis and neuronal differentiation. 2. **Immune function**: KMT2A plays a crucial role in the development and function of immune cells, including T cells, B cells, and dendritic cells. 3. **Circadian regulation**: KMT2A is involved in the regulation of circadian gene expression, influencing the body's internal clock. 4. **Neurological function**: KMT2A is expressed in the brain and regulates the expression of genes involved in neuronal development, synaptic plasticity, and learning. **Clinical Significance:** KMT2A's dysregulation has been implicated in various diseases, including: 1. **Leukemia**: KMT2A is often mutated or deleted in leukemia, leading to the development of aggressive T-cell malignancies. 2. **Neurological disorders**: KMT2A mutations have been linked to neurological disorders, such as intellectual disability and epilepsy. 3. **Immune disorders**: KMT2A's dysregulation can lead to impaired immune function, increasing the risk of infections and autoimmune diseases. In conclusion, KMT2A is a complex and multifunctional gene that plays a critical role in epigenetic regulation, immune function, and developmental processes. Its dysregulation can have significant clinical implications, highlighting the need for further research into the molecular mechanisms underlying KMT2A's functions and the development of targeted therapies for diseases associated with its dysregulation.

Genular Protein ID: 79887688

Symbol: KMT2A_HUMAN

Name: Histone-lysine N-methyltransferase 2A

UniProtKB Accession Codes:

Q03164 E9PQG7 Q13743 Q13744 Q14845 Q16364 Q59FF2 Q6UBD1 Q9HBJ3 Q9UD94 Q9UMA3

Database IDs:

AGR 1 Antibodypedia 1 BMRB 1 Bgee 1 BindingDB 1 BioCyc 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CDD 6 CORUM 1 CTD 1 CarbonylDB 1 ChEBI 32 ChEMBL 1 ChiTaRS 1 ComplexPortal 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DisProt 1 EC 1 ELM 1 EMBL 50 EMDB 11 Ensembl 3 EvolutionaryTrace 1 ExpressionAtlas 1 GO 40 Gene3D 5 GeneCards 1 GeneReviews 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 IDEAL 1 InParanoid 1 IntAct 1 InterPro 19 KEGG 1 MANE-Select 1 MIM 3 MINT 1 MalaCards 1 MassIVE 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 7 OrthoDB 1 PANTHER 2 PDB 56 PDBsum 56 PIR 3 PIRSF 1 PRO 1 PROSITE 9 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 6 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 3 Pumba 1 RNAct 1 Reactome 5 RefSeq 2 Rhea 12 SASBDB 1 SIGNOR 1 SMART 6 SMR 1 STRING 1 SUPFAM 3 SignaLink 1 SwissPalm 1 TreeFam 1 UCSC 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 1423624

Title: Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias.

PubMed ID: 1423624

DOI: 10.1016/0092-8674(92)90602-9

PubMed ID: 8703835

Title: Exon/intron structure of the human ALL-1 (MLL) gene involved in translocations to chromosomal region 11q23 and acute leukaemias.

PubMed ID: 8703835

DOI: 10.1046/j.1365-2141.1996.d01-1748.x

PubMed ID: 16554811

Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.

PubMed ID: 16554811

DOI: 10.1038/nature04632

PubMed ID: 8378076

Title: Two distinct portions of LTG19/ENL at 19p13 are involved in t(11;19) leukemia.

PubMed ID: 8378076

PubMed ID: 1423625

Title: The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene.

PubMed ID: 1423625

DOI: 10.1016/0092-8674(92)90603-a

PubMed ID: 1303259

Title: A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias.

PubMed ID: 1303259

DOI: 10.1038/ng1092-113

PubMed ID: 8401594

Title:

PubMed ID: 8401594

DOI: 10.1038/ng0893-431

PubMed ID: 7794749

Title: Molecular analysis of the chromosomal breakpoint and fusion transcripts in the acute lymphoblastic SEM cell line with chromosomal translocation t(4;11).

PubMed ID: 7794749

DOI: 10.1111/j.1365-2141.1995.tb05151.x

PubMed ID: 7598802

Title: The human MLL gene: nucleotide sequence, homology to the Drosophila trx zinc-finger domain, and alternative splicing.

PubMed ID: 7598802

DOI: 10.1089/dna.1995.14.475

PubMed ID: 8162575

Title: Sequence analysis of the breakpoint cluster region in the ALL-1 gene involved in acute leukemia.

PubMed ID: 8162575

PubMed ID: 10706619

Title: Detection of leukemia-associated MLL-GAS7 translocation early during chemotherapy with DNA topoisomerase II inhibitors.

PubMed ID: 10706619

DOI: 10.1073/pnas.050397097

PubMed ID: 8414518

Title: A method for identifying genes within yeast artificial chromosomes: application to isolation of MLL fusion cDNAs from acute leukaemia translocations.

PubMed ID: 8414518

PubMed ID: 12482972

Title: Proteolytic cleavage of MLL generates a complex of N- and C-terminal fragments that confers protein stability and subnuclear localization.

PubMed ID: 12482972

DOI: 10.1128/mcb.23.1.186-194.2003

PubMed ID: 8950979

Title: Fusion of the MLL gene with two different genes, AF-6 and AF-5alpha, by a complex translocation involving chromosomes 5, 6, 8 and 11 in infant leukemia.

PubMed ID: 8950979

PubMed ID: 9694699

Title: ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene in acute myeloid leukemia with t(10;11)(p11.2;q23).

PubMed ID: 9694699

PubMed ID: 9537414

Title: Association of SET domain and myotubularin-related proteins modulates growth control.

PubMed ID: 9537414

DOI: 10.1038/ng0498-331

PubMed ID: 10490642

Title: Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteins.

PubMed ID: 10490642

DOI: 10.1128/mcb.19.10.7050

PubMed ID: 10588740

Title: AF5q31, a newly identified AF4-related gene, is fused to MLL in infant acute lymphoblastic leukemia with ins(5;11)(q31;q13q23).

PubMed ID: 10588740

DOI: 10.1073/pnas.96.25.14535

PubMed ID: 10648423

Title: Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed lineage leukemia protein in a therapy-related leukemia with t(3;11)(p21;q23).

PubMed ID: 10648423

PubMed ID: 11110714

Title: t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (guanosine 5-prime monophosphate synthetase) gene.

PubMed ID: 11110714

PubMed ID: 11433529

Title: Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23).

PubMed ID: 11433529

DOI: 10.1002/gcc.1157

PubMed ID: 12124344

Title: LCX, leukemia-associated protein with a CXXC domain, is fused to MLL in acute myeloid leukemia with trilineage dysplasia having t(10;11)(q22;q23).

PubMed ID: 12124344

PubMed ID: 12453419

Title: ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation.

PubMed ID: 12453419

DOI: 10.1016/s1097-2765(02)00740-2

PubMed ID: 14636557

Title: Taspase1: a threonine aspartase required for cleavage of MLL and proper HOX gene expression.

PubMed ID: 14636557

DOI: 10.1016/s0092-8674(03)00816-x

PubMed ID: 12618766

Title: A t(11;15) fuses MLL to two different genes, AF15q14 and a novel gene MPFYVE on chromosome 15.

PubMed ID: 12618766

DOI: 10.1038/sj.onc.1206273

PubMed ID: 12618768

Title: Characterization of the MLL partner gene AF15q14 involved in t(11;15)(q23;q14).

PubMed ID: 12618768

DOI: 10.1038/sj.onc.1206272

PubMed ID: 14978793

Title: Identification of a novel RAS GTPase-activating protein (RASGAP) gene at 9q34 as an MLL fusion partner in a patient with de novo acute myeloid leukemia.

PubMed ID: 14978793

DOI: 10.1002/gcc.20004

PubMed ID: 14999297

Title: FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23).

PubMed ID: 14999297

DOI: 10.1038/sj.leu.2403334

PubMed ID: 15199122

Title: Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression.

PubMed ID: 15199122

DOI: 10.1128/mcb.24.13.5639-5649.2004

PubMed ID: 16061630

Title: AF4p12, a human homologue to the furry gene of Drosophila, as a novel MLL fusion partner.

PubMed ID: 16061630

DOI: 10.1158/0008-5472.can-05-1325

PubMed ID: 15960975

Title: Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.

PubMed ID: 15960975

DOI: 10.1016/j.cell.2005.04.031

PubMed ID: 17467953

Title: Nine-amino-acid transactivation domain: establishment and prediction utilities.

PubMed ID: 17467953

DOI: 10.1016/j.ygeno.2007.02.003

PubMed ID: 17500065

Title: PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex.

PubMed ID: 17500065

DOI: 10.1074/jbc.m701574200

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19556245

Title: On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex.

PubMed ID: 19556245

DOI: 10.1074/jbc.m109.014498

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23508102

Title: Quantitative dissection and stoichiometry determination of the human SET1/MLL histone methyltransferase complexes.

PubMed ID: 23508102

DOI: 10.1128/mcb.01742-12

PubMed ID: 25593309

Title: Screen identifies bromodomain protein ZMYND8 in chromatin recognition of transcription-associated DNA damage that promotes homologous recombination.

PubMed ID: 25593309

DOI: 10.1101/gad.252189.114

PubMed ID: 25561738

Title: Biochemical reconstitution and phylogenetic comparison of human SET1 family core complexes involved in histone methylation.

PubMed ID: 25561738

DOI: 10.1074/jbc.m114.627646

PubMed ID: 22795537

Title: De novo mutations in MLL cause Wiedemann-Steiner syndrome.

PubMed ID: 22795537

DOI: 10.1016/j.ajhg.2012.06.008

PubMed ID: 23178126

Title: Microcephaly gene links trithorax and REST/NRSF to control neural stem cell proliferation and differentiation.

PubMed ID: 23178126

DOI: 10.1016/j.cell.2012.10.043

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24235145

Title: Automethylation activities within the mixed lineage leukemia-1 (MLL1) core complex reveal evidence supporting a 'two-active site' model for multiple histone H3 lysine 4 methylation.

PubMed ID: 24235145

DOI: 10.1074/jbc.m113.501064

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 34850113

Title: MLL1 is regulated by KSHV LANA and is important for virus latency.

PubMed ID: 34850113

DOI: 10.1093/nar/gkab1094

PubMed ID: 16990798

Title: Solution structure of the nonmethyl-CpG-binding CXXC domain of the leukaemia-associated MLL histone methyltransferase.

PubMed ID: 16990798

DOI: 10.1038/sj.emboj.7601340

PubMed ID: 16253272

Title: Structural basis for cooperative transcription factor binding to the CBP coactivator.

PubMed ID: 16253272

DOI: 10.1016/j.jmb.2005.09.059

PubMed ID: 18829459

Title: Structure of WDR5 bound to mixed lineage leukemia protein-1 peptide.

PubMed ID: 18829459

DOI: 10.1074/jbc.c800164200

PubMed ID: 18840606

Title: WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket.

PubMed ID: 18840606

DOI: 10.1074/jbc.m806900200

PubMed ID: 19187761

Title: Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks.

PubMed ID: 19187761

DOI: 10.1016/j.molcel.2008.12.029

PubMed ID: 20677832

Title: The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-mediated activation and repression.

PubMed ID: 20677832

DOI: 10.1021/bi1009387

PubMed ID: 20541251

Title: Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression.

PubMed ID: 20541251

DOI: 10.1016/j.cell.2010.05.016

PubMed ID: 20010842

Title: Structure of the MLL CXXC domain-DNA complex and its functional role in MLL-AF9 leukemia.

PubMed ID: 20010842

DOI: 10.1038/nsmb.1714

PubMed ID: 21220120

Title: Structural and biochemical insights into MLL1 core complex assembly.

PubMed ID: 21220120

DOI: 10.1016/j.str.2010.09.022

PubMed ID: 22936661

Title: Structural insights into inhibition of the bivalent menin-MLL interaction by small molecules in leukemia.

PubMed ID: 22936661

DOI: 10.1182/blood-2012-05-429274

PubMed ID: 22665483

Title: Structural basis for WDR5 interaction (Win) motif recognition in human SET1 family histone methyltransferases.

PubMed ID: 22665483

DOI: 10.1074/jbc.m112.364125

PubMed ID: 22327296

Title: The same pocket in menin binds both MLL and JUND but has opposite effects on transcription.

PubMed ID: 22327296

DOI: 10.1038/nature10806

PubMed ID: 23651431

Title: Allosteric communication in the KIX domain proceeds through dynamic repacking of the hydrophobic core.

PubMed ID: 23651431

DOI: 10.1021/cb4002188

PubMed ID: 25305204

Title: The same site on the integrase-binding domain of lens epithelium-derived growth factor is a therapeutic target for MLL leukemia and HIV.

PubMed ID: 25305204

DOI: 10.1182/blood-2014-01-550079

PubMed ID: 25082813

Title: Validation and structural characterization of the LEDGF/p75-MLL interface as a new target for the treatment of MLL-dependent leukemia.

PubMed ID: 25082813

DOI: 10.1158/0008-5472.can-13-3602

PubMed ID: 26886794

Title: Structural basis for activity regulation of MLL family methyltransferases.

PubMed ID: 26886794

DOI: 10.1038/nature16952

PubMed ID: 29997176

Title: Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-dependent phosphorylation.

PubMed ID: 29997176

DOI: 10.1073/pnas.1803909115

PubMed ID: 29276034

Title: DNA Sequence Recognition of Human CXXC Domains and Their Structural Determinants.

PubMed ID: 29276034

DOI: 10.1016/j.str.2017.11.022

Sequence Information:

  • Length: 3969
  • Mass: 431764
  • Checksum: 1150F37EAB1430D3
  • Sequence:
    • MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG PGAPPSPPAV 
AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS SGPALLRVGP GFDAALQVSA 
AIGTNLRRFR AVFGESGGGG GSGEDEQFLG FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR 
SGSDRNSAIL SDPSVFSPLN KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD 
ISELPKGNKE DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV 
RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ SPRRIKPVRI 
IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK TQVKNIRQFI MPVVSAISSR 
IIKTPRRFIE DEDYDPPIKI ARLESTPNSR FSAPSCGSSE KSSAASQHSS QMSSDSSRSS 
SPSVDTSTDS QASEEIQVLP EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS 
RTTKKLSTLQ SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS 
TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN FRPPPLTPED 
VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP RFTPSEAHSR IFESVTLPSN 
RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS PSHSMRTRSG RLSSSELSPL TPPSSVSSSL 
SISVSPLATS ALNPTFTFPS HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT 
PGSQTERGRN KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ 
SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL GDTTAVKTKI 
LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK HSTSSIGSML AQADKLPMTD 
KRVASLLKKA KAQLCKIEKS KSLKQTDQPK AQGQESDSSE TSVRGPRIKH VCRRAAVALG 
RKRAVFPDDM PTLSALPWEE REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA 
PQEPPVKKGR RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM 
PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE DPAPKKSSSE 
PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ PALVIPPQPP TTGPPRKEVP 
KTTPSEPKKK QPPPPESGPE QSKQKKVAPR PSIPVKQKPK EKEKPPPVNK QENAGTLNIL 
STLSNGNSSK QKIPADGVHR IRVDFKEDCE AENVWEMGGL GILTSVPITP RVVCFLCASS 
GHVEFVYCQV CCEPFHKFCL EENERPLEDQ LENWCCRRCK FCHVCGRQHQ ATKQLLECNK 
CRNSYHPECL GPNYPTKPTK KKKVWICTKC VRCKSCGSTT PGKGWDAQWS HDFSLCHDCA 
KLFAKGNFCP LCDKCYDDDD YESKMMQCGK CDRWVHSKCE NLSDEMYEIL SNLPESVAYT 
CVNCTERHPA EWRLALEKEL QISLKQVLTA LLNSRTTSHL LRYRQAAKPP DLNPETEESI 
PSRSSPEGPD PPVLTEVSKQ DDQQPLDLEG VKRKMDQGNY TSVLEFSDDI VKIIQAAINS 
DGGQPEIKKA NSMVKSFFIR QMERVFPWFS VKKSRFWEPN KVSSNSGMLP NAVLPPSLDH 
NYAQWQEREE NSHTEQPPLM KKIIPAPKPK GPGEPDSPTP LHPPTPPILS TDRSREDSPE 
LNPPPGIEDN RQCALCLTYG DDSANDAGRL LYIGQNEWTH VNCALWSAEV FEDDDGSLKN 
VHMAVIRGKQ LRCEFCQKPG ATVGCCLTSC TSNYHFMCSR AKNCVFLDDK KVYCQRHRDL 
IKGEVVPENG FEVFRRVFVD FEGISLRRKF LNGLEPENIH MMIGSMTIDC LGILNDLSDC 
EDKLFPIGYQ CSRVYWSTTD ARKRCVYTCK IVECRPPVVE PDINSTVEHD ENRTIAHSPT 
SFTESSSKES QNTAEIISPP SPDRPPHSQT SGSCYYHVIS KVPRIRTPSY SPTQRSPGCR 
PLPSAGSPTP TTHEIVTVGD PLLSSGLRSI GSRRHSTSSL SPQRSKLRIM SPMRTGNTYS 
RNNVSSVSTT GTATDLESSA KVVDHVLGPL NSSTSLGQNT STSSNLQRTV VTVGNKNSHL 
DGSSSSEMKQ SSASDLVSKS SSLKGEKTKV LSSKSSEGSA HNVAYPGIPK LAPQVHNTTS 
RELNVSKIGS FAEPSSVSFS SKEALSFPHL HLRGQRNDRD QHTDSTQSAN SSPDEDTEVK 
TLKLSGMSNR SSIINEHMGS SSRDRRQKGK KSCKETFKEK HSSKSFLEPG QVTTGEEGNL 
KPEFMDEVLT PEYMGQRPCN NVSSDKIGDK GLSMPGVPKA PPMQVEGSAK ELQAPRKRTV 
KVTLTPLKME NESQSKNALK ESSPASPLQI ESTSPTEPIS ASENPGDGPV AQPSPNNTSC 
QDSQSNNYQN LPVQDRNLML PDGPKPQEDG SFKRRYPRRS ARARSNMFFG LTPLYGVRSY 
GEEDIPFYSS STGKKRGKRS AEGQVDGADD LSTSDEDDLY YYNFTRTVIS SGGEERLASH 
NLFREEEQCD LPKISQLDGV DDGTESDTSV TATTRKSSQI PKRNGKENGT ENLKIDRPED 
AGEKEHVTKS SVGHKNEPKM DNCHSVSRVK TQGQDSLEAQ LSSLESSRRV HTSTPSDKNL 
LDTYNTELLK SDSDNNNSDD CGNILPSDIM DFVLKNTPSM QALGESPESS SSELLNLGEG 
LGLDSNREKD MGLFEVFSQQ LPTTEPVDSS VSSSISAEEQ FELPLELPSD LSVLTTRSPT 
VPSQNPSRLA VISDSGEKRV TITEKSVASS ESDPALLSPG VDPTPEGHMT PDHFIQGHMD 
ADHISSPPCG SVEQGHGNNQ DLTRNSSTPG LQVPVSPTVP IQNQKYVPNS TDSPGPSQIS 
NAAVQTTPPH LKPATEKLIV VNQNMQPLYV LQTLPNGVTQ KIQLTSSVSS TPSVMETNTS 
VLGPMGGGLT LTTGLNPSLP TSQSLFPSAS KGLLPMSHHQ HLHSFPAATQ SSFPPNISNP 
PSGLLIGVQP PPDPQLLVSE SSQRTDLSTT VATPSSGLKK RPISRLQTRK NKKLAPSSTP 
SNIAPSDVVS NMTLINFTPS QLPNHPSLLD LGSLNTSSHR TVPNIIKRSK SSIMYFEPAP 
LLPQSVGGTA ATAAGTSTIS QDTSHLTSGS VSGLASSSSV LNVVSMQTTT TPTSSASVPG 
HVTLTNPRLL GTPDIGSISN LLIKASQQSL GIQDQPVALP PSSGMFPQLG TSQTPSTAAI 
TAASSICVLP STQTTGITAA SPSGEADEHY QLQHVNQLLA SKTGIHSSQR DLDSASGPQV 
SNFTQTVDAP NSMGLEQNKA LSSAVQASPT SPGGSPSSPS SGQRSASPSV PGPTKPKPKT 
KRFQLPLDKG NGKKHKVSHL RTSSSEAHIP DQETTSLTSG TGTPGAEAEQ QDTASVEQSS 
QKECGQPAGQ VAVLPEVQVT QNPANEQESA EPKTVEEEES NFSSPLMLWL QQEQKRKESI 
TEKKPKKGLV FEISSDDGFQ ICAESIEDAW KSLTDKVQEA RSNARLKQLS FAGVNGLRML 
GILHDAVVFL IEQLSGAKHC RNYKFRFHKP EEANEPPLNP HGSARAEVHL RKSAFDMFNF 
LASKHRQPPE YNPNDEEEEE VQLKSARRAT SMDLPMPMRF RHLKKTSKEA VGVYRSPIHG 
RGLFCKRNID AGEMVIEYAG NVIRSIQTDK REKYYDSKGI GCYMFRIDDS EVVDATMHGN 
AARFINHSCE PNCYSRVINI DGQKHIVIFA MRKIYRGEEL TYDYKFPIED ASNKLPCNCG 
AKKCRKFLN

Genular Protein ID: 1869457149

Symbol: E9PR05_HUMAN

Name: N/A

UniProtKB Accession Codes:

E9PR05

Database IDs:

ARBA 14 Antibodypedia 1 Bgee 1 CDD 6 CTD 1 ChEBI 19 ChiTaRS 1 EC 1 EMBL 2 Ensembl 2 ExpressionAtlas 1 GO 8 Gene3D 5 GeneTree 1 HGNC 1 HOGENOM 1 InterPro 19 MassIVE 1 NCBI Taxonomy 1 PANTHER 2 PIRNR 1 PIRSF 1 PIRSR 2 PROSITE 14 PROSITE-ProRule 2 PeptideAtlas 2 Pfam 6 Proteomes 2 ProteomicsDB 2 RefSeq 1 Rhea 7 SAM 1 SMART 6 SMR 1 SUPFAM 3 UCSC 1 VEuPathDB 1

Citations:

PubMed ID: 11237011

Title: Initial sequencing and analysis of the human genome.

PubMed ID: 11237011

DOI: 10.1038/35057062

PubMed ID: 15496913

Title: Finishing the euchromatic sequence of the human genome.

PubMed ID: 15496913

DOI: 10.1038/nature03001

PubMed ID: 16554811

Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.

PubMed ID: 16554811

DOI: 10.1038/nature04632

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

Sequence Information:

  • Length: 4005
  • Mass: 436001
  • Checksum: 57FF6014C350A136
  • Sequence:
    • MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG PGAPPSPPAV 
AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS SGPALLRVGP GFDAALQVSA 
AIGTNLRRFR AVFGESGGGG GSGELTTQIP CSWRTKGHIH DKKTEPFRLL AWSWCLNDEQ 
FLGFGSDEEV RVRSPTRSPS VKTSPRKPRG RPRSGSDRNS AILSDPSVFS PLNKSETKSG 
DKIKKKDSKS IEKKRGRPPT FPGVKIKITH GKDISELPKG NKEDSLKKIK RTPSATFQQA 
TKIKKLRAGK LSPLKSKFKT GKLQIGRKGV QIVRRRGRPP STERIKTPSG LLINSELEKP 
QKVRKDKEGT PPLTKEDKTV VRQSPRRIKP VRIIPSSKRT DATIAKQLLQ RAKKGAQKKI 
EKEAAQLQGR KVKTQVKNIR QFIMPVVSAI SSRIIKTPRR FIEDEDYDPP IKIARLESTP 
NSRFSAPSCG SSEKSSAASQ HSSQMSSDSS RSSSPSVDTS TDSQASEEIQ VLPEERSDTP 
EVHPPLPISQ SPENESNDRR SRRYSVSERS FGSRTTKKLS TLQSAPQQQT SSSPPPPLLT 
PPPPLQPASS ISDHTPWLMP PTIPLASPFL PASTAPMQGK RKSILREPTF RWTSLKHSRS 
EPQYFSSAKY AKEGLIRKPI FDNFRPPPLT PEDVGFASGF SASGTAASAR LFSPLHSGTR 
FDMHKRSPLL RAPRFTPSEA HSRIFESVTL PSNRTSAGTS SSGVSNRKRK RKVFSPIRSE 
PRSPSHSMRT RSGRLSSSEL SPLTPPSSVS SSLSISVSPL ATSALNPTFT FPSHSLTQSG 
ESAEKNQRPR KQTSAPAEPF SSSSPTPLFP WFTPGSQTER GRNKDKAPEE LSKDRDADKS 
VEKDKSRERD REREKENKRE SRKEKRKKGS EIQSSSALYP VGRVSKEKVV GEDVATSSSA 
KKATGRKKSS SHDSGTDITS VTLGDTTAVK TKILIKKGRG NLEKTNLDLG PTAPSLEKEK 
TLCLSTPSSS TVKHSTSSIG SMLAQADKLP MTDKRVASLL KKAKAQLCKI EKSKSLKQTD 
QPKAQGQESD SSETSVRGPR IKHVCRRAAV ALGRKRAVFP DDMPTLSALP WEEREKILSS 
MGNDDKSSIA GSEDAEPLAP PIKPIKPVTR NKAPQEPPVK KGRRSRRCGQ CPGCQVPEDC 
GVCTNCLDKP KFGGRNIKKQ CCKMRKCQNL QWMPSKAYLQ KQAKAVKKKE KKSKTSEKKD 
SKESSVVKNV VDSSQKPTPS AREDPAPKKS SSEPPPRKPV EEKSEEGNVS APGPESKQAT 
TPASRKSSKQ VSQPALVIPP QPPTTGPPRK EVPKTTPSEP KKKQPPPPES GPEQSKQKKV 
APRPSIPVKQ KPKEKEKPPP VNKQENAGTL NILSTLSNGN SSKQKIPADG VHRIRVDFKE 
DCEAENVWEM GGLGILTSVP ITPRVVCFLC ASSGHVEFVY CQVCCEPFHK FCLEENERPL 
EDQLENWCCR RCKFCHVCGR QHQATKQLLE CNKCRNSYHP ECLGPNYPTK PTKKKKVWIC 
TKCVRCKSCG STTPGKGWDA QWSHDFSLCH DCAKLFAKGN FCPLCDKCYD DDDYESKMMQ 
CGKCDRWVHS KCENLSGTED EMYEILSNLP ESVAYTCVNC TERHPAEWRL ALEKELQISL 
KQVLTALLNS RTTSHLLRYR QAAKPPDLNP ETEESIPSRS SPEGPDPPVL TEVSKQDDQQ 
PLDLEGVKRK MDQGNYTSVL EFSDDIVKII QAAINSDGGQ PEIKKANSMV KSFFIRQMER 
VFPWFSVKKS RFWEPNKVSS NSGMLPNAVL PPSLDHNYAQ WQEREENSHT EQPPLMKKII 
PAPKPKGPGE PDSPTPLHPP TPPILSTDRS REDSPELNPP PGIEDNRQCA LCLTYGDDSA 
NDAGRLLYIG QNEWTHVNCA LWSAEVFEDD DGSLKNVHMA VIRGKQLRCE FCQKPGATVG 
CCLTSCTSNY HFMCSRAKNC VFLDDKKVYC QRHRDLIKGE VVPENGFEVF RRVFVDFEGI 
SLRRKFLNGL EPENIHMMIG SMTIDCLGIL NDLSDCEDKL FPIGYQCSRV YWSTTDARKR 
CVYTCKIVEC RPPVVEPDIN STVEHDENRT IAHSPTSFTE SSSKESQNTA EIISPPSPDR 
PPHSQTSGSC YYHVISKVPR IRTPSYSPTQ RSPGCRPLPS AGSPTPTTHE IVTVGDPLLS 
SGLRSIGSRR HSTSSLSPQR SKLRIMSPMR TGNTYSRNNV SSVSTTGTAT DLESSAKVVD 
HVLGPLNSST SLGQNTSTSS NLQRTVVTVG NKNSHLDGSS SSEMKQSSAS DLVSKSSSLK 
GEKTKVLSSK SSEGSAHNVA YPGIPKLAPQ VHNTTSRELN VSKIGSFAEP SSVSFSSKEA 
LSFPHLHLRG QRNDRDQHTD STQSANSSPD EDTEVKTLKL SGMSNRSSII NEHMGSSSRD 
RRQKGKKSCK ETFKEKHSSK SFLEPGQVTT GEEGNLKPEF MDEVLTPEYM GQRPCNNVSS 
DKIGDKGLSM PGVPKAPPMQ VEGSAKELQA PRKRTVKVTL TPLKMENESQ SKNALKESSP 
ASPLQIESTS PTEPISASEN PGDGPVAQPS PNNTSCQDSQ SNNYQNLPVQ DRNLMLPDGP 
KPQEDGSFKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED IPFYSSSTGK KRGKRSAEGQ 
VDGADDLSTS DEDDLYYYNF TRTVISSGGE ERLASHNLFR EEEQCDLPKI SQLDGVDDGT 
ESDTSVTATT RKSSQIPKRN GKENGTENLK IDRPEDAGEK EHVTKSSVGH KNEPKMDNCH 
SVSRVKTQGQ DSLEAQLSSL ESSRRVHTST PSDKNLLDTY NTELLKSDSD NNNSDDCGNI 
LPSDIMDFVL KNTPSMQALG ESPESSSSEL LNLGEGLGLD SNREKDMGLF EVFSQQLPTT 
EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ NPSRLAVISD SGEKRVTITE 
KSVASSESDP ALLSPGVDPT PEGHMTPDHF IQGHMDADHI SSPPCGSVEQ GHGNNQDLTR 
NSSTPGLQVP VSPTVPIQNQ KYVPNSTDSP GPSQISNAAV QTTPPHLKPA TEKLIVVNQN 
MQPLYVLQTL PNGVTQKIQL TSSVSSTPSV METNTSVLGP MGGGLTLTTG LNPSLPTSQS 
LFPSASKGLL PMSHHQHLHS FPAATQSSFP PNISNPPSGL LIGVQPPPDP QLLVSESSQR 
TDLSTTVATP SSGLKKRPIS RLQTRKNKKL APSSTPSNIA PSDVVSNMTL INFTPSQLPN 
HPSLLDLGSL NTSSHRTVPN IIKRSKSSIM YFEPAPLLPQ SVGGTAATAA GTSTISQDTS 
HLTSGSVSGL ASSSSVLNVV SMQTTTTPTS SASVPGHVTL TNPRLLGTPD IGSISNLLIK 
ASQQSLGIQD QPVALPPSSG MFPQLGTSQT PSTAAITAAS SICVLPSTQT TGITAASPSG 
EADEHYQLQH VNQLLASKTG IHSSQRDLDS ASGPQVSNFT QTVDAPNSMG LEQNKALSSA 
VQASPTSPGG SPSSPSSGQR SASPSVPGPT KPKPKTKRFQ LPLDKGNGKK HKVSHLRTSS 
SEAHIPDQET TSLTSGTGTP GAEAEQQDTA SVEQSSQKEC GQPAGQVAVL PEVQVTQNPA 
NEQESAEPKT VEEEESNFSS PLMLWLQQEQ KRKESITEKK PKKGLVFEIS SDDGFQICAE 
SIEDAWKSLT DKVQEARSNA RLKQLSFAGV NGLRMLGILH DAVVFLIEQL SGAKHCRNYK 
FRFHKPEEAN EPPLNPHGSA RAEVHLRKSA FDMFNFLASK HRQPPEYNPN DEEEEEVQLK 
SARRATSMDL PMPMRFRHLK KTSKEAVGVY RSPIHGRGLF CKRNIDAGEM VIEYAGNVIR 
SIQTDKREKY YDSKGIGCYM FRIDDSEVVD ATMHGNAARF INHSCEPNCY SRVINIDGQK 
HIVIFAMRKI YRGEELTYDY KFPIEDASNK LPCNCGAKKC RKFLN

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.