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MLL2 MLL2 PAXIP1 PAXIP1 PER1 PER1 HIST1H3A HIST1H3A NCOA6 NCOA6 KDM6A KDM6A PER2 PER2 CXXC1 CXXC1 ASH2L ASH2L CSE1L CSE1L UBC UBC SETD1A SETD1A MLL4 MLL4 USP1 USP1 WDR5 WDR5 RBBP5 RBBP5 SETD1B SETD1B UNC45A UNC45A HCFC1 HCFC1 CHD8 CHD8 MLLT1 MLLT1 MLL MLL PPP1CB PPP1CB ENSG00000267140 ENSG00000267140 KANSL1 KANSL1 KANSL3 KANSL3
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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small nodes:
protein of unknown 3D structure
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large nodes:
some 3D structure is known or predicted
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query proteins and first shell of interactors
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white nodes:
second shell of interactors
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Edges represent protein-protein associations
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experimentally determined
Predicted Interactions
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textmining
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MLL4Histone-lysine N-methyltransferase MLL4 ; 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 r [...] (2715 aa)
MLLT1myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 1; Component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA (559 aa)
PER2period homolog 2 (Drosophila); Component of the circadian clock mechanism which is essential for generating circadian rhythms. Negative element in the circadian transcriptional loop. Influences clock function by interacting with other circadian regulatory proteins and transporting them to the nucleus. Negatively regulates CLOCK|NPAS2-BMAL1|BMAL2-induced transactivation (By similarity) (1255 aa)
KANSL1KAT8 regulatory NSL complex subunit 1; As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription (1105 aa)
SETD1ASET domain containing 1A; Histone methyltransferase that specifically methylates ’Lys-4’ of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring ’Lys- 9’ residue is already methylated. H3 ’Lys-4’ methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1B suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression (1707 aa)
CSE1LCSE1 chromosome segregation 1-like (yeast) (971 aa)
RBBP5retinoblastoma binding protein 5; In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 ’Lys-4’ methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at ’Lys-4’ of histone H3. Histone H3 ’Lys-4’ methylation represents a specific tag for epigenetic transcriptional activation (538 aa)
SETD1BSET domain containing 1B; Histone methyltransferase that specifically methylates ’Lys-4’ of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring ’Lys- 9’ residue is already methylated. H3 ’Lys-4’ methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates ’Lys-4’ of histone H3 in vitro (1923 aa)
PPP1CBprotein phosphatase 1, catalytic subunit, beta isozyme; Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during [...] (327 aa)
MLL2myeloid/lymphoid or mixed-lineage leukemia 2; Histone methyltransferase. Methylates ’Lys-4’ of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription (5537 aa)
HCFC1host cell factor C1 (VP16-accessory protein); Involved in control of the cell cycle. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. Tethers the chromatin modifying Set1/Ash2 histone H3 ’Lys-4’ methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional a [...] (2035 aa)
PER1period homolog 1 (Drosophila); Component of the circadian clock mechanism which is essential for generating circadian rhythms. Negative element in the circadian transcriptional loop. Influences clock function by interacting with other circadian regulatory proteins and transporting them to the nucleus. Negatively regulates CLOCK|NPAS2-BMAL1|BMAL2-induced transactivation. Can bind heme (By similarity) (1290 aa)
ASH2Lash2 (absent, small, or homeotic)-like (Drosophila); Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates ’Lys-4’ of histone H3, but not if the neighboring ’Lys-9’ residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at ’Lys-4’ of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis (628 aa)
USP1ubiquitin specific peptidase 1; Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2. Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity (785 aa)
UBCubiquitin C (685 aa)
HIST1H3Ahistone cluster 1, H3a (136 aa)
WDR5WD repeat domain 5; Contributes to histone modification. May position the N- terminus of histone H3 for efficient trimethylation at ’Lys-4’. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at ’Lys-4’ of histone H3. H3 ’Lys-4’ methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation (334 aa)
NCOA6nuclear receptor coactivator 6; Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Coactivates expression in an agonist- and AF2-dependent manner. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ERs), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Probably functions as a general coactivator, rather than just a nuclear receptor coactivator. May also be involved in the coactivation of the NF-kappa-B pathway. M [...] (2063 aa)
KDM6Alysine (K)-specific demethylase 6A; Histone demethylase that specifically demethylates ’Lys- 27’ of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated but not monomethylated H3 ’Lys-27’. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Demethylation of ’Lys-27’ of histone H3 is concomitant with methylation of ’Lys-4’ of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A (1401 aa)
CHD8chromodomain helicase DNA binding protein 8 (2581 aa)
PAXIP1PAX interacting (with transcription-activation domain) protein 1; Involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. Plays a role in early development. In DNA damage response is required for cell survival after ionizing radiation. In vitro shown to be involved in the homologous recombination mechanism for the repair of double-strand breaks (DSBs). Its localization to DNA damage foci requires RNF8 and UBE2N. Recruits TP53BP1 to DNA damage foci and, at least in particular repair processes, effective DNA damage response app [...] (1069 aa)
CXXC1CXXC finger protein 1; Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG (660 aa)
KANSL3KAT8 regulatory NSL complex subunit 3 (878 aa)
UNC45Aunc-45 homolog A (C. elegans); Acts as co-chaperone for HSP90. Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell. May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity) (944 aa)
MLLmyeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila) (3972 aa)
ENSG00000267140IES6 homolog; Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair (123 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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