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SETDB2 SETDB2 GTPBP3 GTPBP3 GBE1 GBE1 SMYD5 SMYD5 SMYD4 SMYD4 SNRPD3 SNRPD3 SMYD1 SMYD1 SNRPA1 SNRPA1 SETD8 SETD8 UHRF2 UHRF2 MLL5 MLL5 TBC1D2B TBC1D2B SMYD2 SMYD2 SETDB1 SETDB1 CBX3 CBX3 TRDMT1 TRDMT1 MLL3 MLL3 ASH1L ASH1L CDY2B CDY2B MPHOSPH8 MPHOSPH8 EZH1 EZH1 MLL2 MLL2 NFRKB NFRKB SETBP1 SETBP1 SETMAR SETMAR
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
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SNRPD3small nuclear ribonucleoprotein D3 polypeptide 18kDa; Appears to function in the U7 snRNP complex that is involved in histone 3’-end processing. Binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner (126 aa)
SNRPA1small nuclear ribonucleoprotein polypeptide A’; This protein is associated with sn-RNP U2. It helps the A’ protein to bind stem loop IV of U2 snRNA (255 aa)
MLL5myeloid/lymphoid or mixed-lineage leukemia 5 (trithorax homolog, Drosophila) (1858 aa)
MLL3myeloid/lymphoid or mixed-lineage leukemia 3; Histone methyltransferase. Methylates ’Lys-4’ of histone H3. H3 ’Lys-4’ methylation represents a specific tag for epigenetic transcriptional activation. Central component of the MLL2/3 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 (4911 aa)
SETDB1SET domain, bifurcated 1; Histone methyltransferase that specifically trimethylates ’Lys-9’ of histone H3. H3 ’Lys-9’ trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 ’Lys-9’ trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone ’Lys-9’ trimethylation. It [...] (1291 aa)
UHRF2ubiquitin-like with PHD and ring finger domains 2, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. Appears to contribute to tumorigenesis (802 aa)
SETBP1SET binding protein 1 (1596 aa)
TBC1D2BTBC1 domain family, member 2B; May act as a GTPase-activating protein (By similarity) (963 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)
SMYD4SET and MYND domain containing 4 (804 aa)
SETDB2SET domain, bifurcated 2; Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates ’Lys-9’ of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to H3K9me3 in both the interspersed repetitive elements and centromere-associated repeats. Plays a role in chromosome condensation and segregation during mitosis (719 aa)
SETD8SET domain containing (lysine methyltransferase) 8; Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates ’Lys-20’ of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome conden [...] (352 aa)
CBX3chromobox homolog 3; Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at ’Lys-9’, leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (183 aa)
GTPBP3GTP binding protein 3 (mitochondrial) (524 aa)
MPHOSPH8M-phase phosphoprotein 8; Involved in transcriptional regulation. Specifically recognizes and binds methylated ’Lys-9’ of histone H3 (H3K9me) and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene. Mediates down-regulation of CDH1 expression (860 aa)
SMYD2SET and MYND domain containing 2; Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 ’Lys-4’ (H3K4me) and dimethylates histone H3 ’Lys-36’ (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates ’Lys-370’ of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates ’Lys-860’ of RB1/RB (433 aa)
TRDMT1tRNA aspartic acid methyltransferase 1; Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp) (391 aa)
CDY2Bchromodomain protein, Y-linked, 2B; May have histone acetyltransferase activity (By similarity) (541 aa)
SETMARSET domain and mariner transposase fusion gene; Histone methyltransferase that methylates ’Lys-4’ and ’Lys-36’ of histone H3, 2 specific tags for epigenetic transcriptional activation. Specifically mediates dimethylation of H3 ’Lys-36’. Has sequence-specific DNA-binding activity and recognizes the 19-mer core of the 5’-terminal inverted repeats (TIRs) of the Hsmar1 element. Has DNA nicking activity. Has in vivo end joining activity and may mediate genomic integration of foreign DNA (684 aa)
SMYD5SMYD family member 5 (418 aa)
ASH1Lash1 (absent, small, or homeotic)-like (Drosophila); Histone methyltransferase specifically methylating ’Lys- 36’ of histone H3 (H3K36me) (2964 aa)
SMYD1SET and MYND domain containing 1; Methylates histone H3 at ’Lys-4’ (H3K4me), seems able to perform both mono-, di-, and trimethylation. Acts as a transcriptional repressor. Essential for cardiomyocyte differentiation and cardiac morphogenesis (490 aa)
EZH1enhancer of zeste homolog 1 (Drosophila) (747 aa)
GBE1glucan (1,4-alpha-), branching enzyme 1; Required for sufficient glycogen accumulation. The alpha 1-6 branches of glycogen play an important role in increasing the solubility of the molecule and, consequently, in reducing the osmotic pressure within cells (702 aa)
NFRKBnuclear factor related to kappaB binding protein; Binds to the DNA consensus sequence 5’-GGGGAATCTCC-3’ (1324 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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