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PPIAL4B PPIAL4B NELL1 NELL1 PPIAL4D PPIAL4D SIRT7 SIRT7 PPIAL4G PPIAL4G ABHD16A ABHD16A PRPF38A PRPF38A NRP1 NRP1 GGPS1 GGPS1 DNAJC19 DNAJC19 SLTM SLTM PPIF PPIF PPIA PPIA SRPK2 SRPK2 HNRNPM HNRNPM ZC3HAV1 ZC3HAV1 SNRNP70 SNRNP70 SFPQ SFPQ PLEC PLEC SNRNP35 SNRNP35 MATR3 MATR3 RANBP2 RANBP2 BMI1 BMI1 PPIAL4A PPIAL4A EED EED SUZ12 SUZ12
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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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some 3D structure is known or predicted
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query proteins and first shell of interactors
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second shell of interactors
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Predicted Interactions
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PPIFpeptidylprolyl isomerase F; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress- i [...] (207 aa)
ZC3HAV1zinc finger CCCH-type, antiviral 1; Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)- specific ribonuclease PARN to remove the poly(A) tail, and the 3’- 5’ exoribonuclease complex exosome to degrade the RNA body from the 3’-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5’-e [...] (902 aa)
PRPF38APRP38 pre-mRNA processing factor 38 (yeast) domain containing A; May be required for pre-mRNA splicing (Potential) (312 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)
NRP1neuropilin 1; The membrane-bound isoform 1 is a receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 isoform of PGF, The VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis (923 aa)
GGPS1geranylgeranyl diphosphate synthase 1; Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins (300 aa)
RANBP2RAN binding protein 2; E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Could also have isomerase or chaperone activity and may bind RNA or DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at ’Lys-490’ which is essential for the proper assembly of PML-NB (3224 aa)
SUZ12suppressor of zeste 12 homolog (Drosophila); Polycomb group (PcG) protein. Component of the PRC2/EED- EZH2 complex, which methylates ’Lys-9’ (H3K9me) and ’Lys-27’ (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A (739 aa)
PLECplectin (4684 aa)
HNRNPMheterogeneous nuclear ribonucleoprotein M; Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines (730 aa)
SIRT7sirtuin 7; NAD-dependent protein deacetylase that specifically mediates deacetylation of histone H3 at ’Lys-18’ (H3K18Ac). In contrast to other histone deacetylases, displays selectivity for a single histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors. SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed pheno [...] (400 aa)
NELL1NEL-like 1 (chicken); Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization (810 aa)
SFPQsplicing factor proline/glutamine-rich; DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation [...] (707 aa)
MATR3matrin 3; May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs (847 aa)
BMI1BMI1 polycomb ring finger oncogene; Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A ’Lys-119’, rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2 (326 aa)
SLTMSAFB-like, transcription modulator (1034 aa)
DNAJC19DnaJ (Hsp40) homolog, subfamily C, member 19; Probable component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity) (116 aa)
SRPK2SRSF protein kinase 2; Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and [...] (699 aa)
ABHD16Aabhydrolase domain containing 16A (558 aa)
PPIAL4Gpeptidylprolyl isomerase A (cyclophilin A)-like 4G; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (164 aa)
SNRNP35small nuclear ribonucleoprotein 35kDa (U11/U12) (251 aa)
PPIApeptidylprolyl isomerase A (cyclophilin A); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (165 aa)
PPIAL4Apeptidylprolyl isomerase A (cyclophilin A)-like 4A (164 aa)
PPIAL4Dpeptidylprolyl isomerase A (cyclophilin A)-like 4D (164 aa)
PPIAL4Bpeptidylprolyl isomerase A (cyclophilin A)-like 4B (164 aa)
SNRNP70small nuclear ribonucleoprotein 70kDa (U1) (437 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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