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APAF1 APAF1 PAFAH1B1 PAFAH1B1 WSB2 WSB2 WDR16 WDR16 TEP1 TEP1 WDR5B WDR5B RBBP5 RBBP5 WDR88 WDR88 ENSG00000259371 ENSG00000259371 ASH2L ASH2L CAMKMT CAMKMT BPTF BPTF NLE1 NLE1 WDR5 WDR5 HIST1H4A HIST1H4A HIST1H3A HIST1H3A PPIE PPIE HIST3H3 HIST3H3 BRD4 BRD4 WHSC1L1 WHSC1L1 EED EED PLOD1 PLOD1 ENSG00000249884 ENSG00000249884 PLOD3 PLOD3 SUPT5H SUPT5H PLOD2 PLOD2
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.
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small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
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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.
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from curated databases
experiment edge
experimentally determined
Predicted Interactions
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gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
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textmining edge
textmining
coexpression edge
co-expression
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protein homology
Your Input:
PLOD1procollagen-lysine, 2-oxoglutarate 5-dioxygenase 1; Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (727 aa)
PLOD3procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3; Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (738 aa)
TEP1telomerase-associated protein 1; Component of the telomerase ribonucleoprotein complex that is essential for the replication of chromosome termini. Also component of the ribonucleoprotein vaults particle, a multi- subunit structure involved in nucleo-cytoplasmic transport. Responsible for the localizing and stabilizing vault RNA (vRNA) association in the vault ribonucleoprotein particle. Binds to TERC (By similarity) (2627 aa)
EEDembryonic ectoderm development; Polycomb group (PcG) protein. Component of the PRC2/EED- EZH2 complex, which methylates ’Lys-9’ and ’Lys-27’ of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes ’Lys-26’ trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 ’Lys-27’, whereas H3 ’Lys-27’ recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby link [...] (441 aa)
BRD4bromodomain containing 4; Plays a role in a process governing chromosomal dynamics during mitosis (By similarity) (1362 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)
PLOD2procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2; Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (758 aa)
BPTFbromodomain PHD finger transcription factor; Histone-binding component of NURF (nucleosome-remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. Specifically recognizes H3 tails trimethylated on ’Lys-4’ (H3K4me3), which mark transcription start sites of virtually all active genes. May also regulate transcription through direct binding to DNA or transcription factors (2920 aa)
WHSC1L1Wolf-Hirschhorn syndrome candidate 1-like 1 (1437 aa)
WSB2WD repeat and SOCS box containing 2; May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity) (404 aa)
WDR5BWD repeat domain 5B; May function as a substrate receptor for CUL4-DDB1 ubiquitin E3 ligase complex (By similarity) (330 aa)
WDR16WD repeat domain 16; May play an essential role in the growth or survival of hepatocellular carcinoma (HCC) (620 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)
WDR88WD repeat domain 88 (472 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)
HIST1H4Ahistone cluster 1, H4a (103 aa)
HIST3H3histone cluster 3, H3; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (136 aa)
PPIEpeptidylprolyl isomerase E (cyclophilin E); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (314 aa)
CAMKMTcalmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin (323 aa)
PAFAH1B1platelet-activating factor acetylhydrolase 1b, regulatory subunit 1 (45kDa); Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet- activating factor (PAF) by removing the acetyl group at the SN-2 position (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated [...] (410 aa)
ENSG00000249884RNF103-CHMP3 readthrough (221 aa)
SUPT5Hsuppressor of Ty 5 homolog (S. cerevisiae); Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promot [...] (1087 aa)
NLE1notchless homolog 1 (Drosophila) (485 aa)
APAF1apoptotic peptidase activating factor 1 (1248 aa)
ENSG00000259371Uncharacterized protein (276 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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