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STRINGSTRING
PTGES3 PTGES3 SSU72 SSU72 PDRG1 PDRG1 ZNF593 ZNF593 SEC23IP SEC23IP PSMD9 PSMD9 OSTF1 OSTF1 XIAP XIAP PXN PXN RNF114 RNF114 TPM1 TPM1 STUB1 STUB1 UBC UBC SMARCD2 SMARCD2 NUDCD2 NUDCD2 SIRT1 SIRT1 SORD SORD PPIL3 PPIL3 SMS SMS TTC1 TTC1 GINS4 GINS4 NUP210 NUP210 PEX19 PEX19 PTMS PTMS SRSF2 SRSF2 PPIAL4A PPIAL4A
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.
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
Your Input:
PDRG1p53 and DNA-damage regulated 1; May play a role in chaperone-mediated protein folding (Potential) (133 aa)
SIRT1sirtuin 1; NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metobolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Se [...] (747 aa)
STUB1STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase; E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates- ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 th [...] (303 aa)
PXNpaxillin; Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion) (591 aa)
TTC1tetratricopeptide repeat domain 1 (292 aa)
RNF114ring finger protein 114; May play a role in spermatogenesis (228 aa)
NUP210nucleoporin 210kDa; Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity (1887 aa)
PTGES3prostaglandin E synthase 3 (cytosolic); Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor- mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes (160 aa)
SORDsorbitol dehydrogenase; Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm (By similarity) (357 aa)
TPM1tropomyosin 1 (alpha) (284 aa)
GINS4GINS complex subunit 4 (Sld5 homolog); The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS4 is important for GINS complex assembly. GINS complex seems to bind preferentially to single-stranded DNA (223 aa)
PPIL3peptidylprolyl isomerase (cyclophilin)-like 3; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing (165 aa)
SSU72SSU72 RNA polymerase II CTD phosphatase homolog (S. cerevisiae); Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK (194 aa)
NUDCD2NudC domain containing 2; May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone (157 aa)
PTMSparathymosin; Parathymosin may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to certain opportunistic infections (102 aa)
OSTF1osteoclast stimulating factor 1; Induces bone resorption, acting probably through a signaling cascade which results in the secretion of factor(s) enhancing osteoclast formation and activity (214 aa)
UBCubiquitin C (685 aa)
XIAPX-linked inhibitor of apoptosis; Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase [...] (497 aa)
SRSF2serine/arginine-rich splicing factor 2; Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5’- and 3’-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre- mRNA. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5’- and 3’-splice site binding components, U1 snRNP and U2AF. Binds to purine-rich RNA sequences, either 5’-AGSAGAGTA-3’ (S=C or G) or [...] (221 aa)
PEX19peroxisomal biogenesis factor 19; Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53 (299 aa)
SEC23IPSEC23 interacting protein; Plays a role in the organization of endoplasmic reticulum exit sites. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P) and phosphatidylinositol 5-phosphate (PI(5)P) (1000 aa)
ZNF593zinc finger protein 593; Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity. Could act either by binding to DNA octamer or by interacting with Oct-2. May also be a modulator of other octamer-binding proteins (134 aa)
SMSspermine synthase; Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM) (366 aa)
SMARCD2SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 2; Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology) (531 aa)
PPIAL4Apeptidylprolyl isomerase A (cyclophilin A)-like 4A (164 aa)
PSMD9proteasome (prosome, macropain) 26S subunit, non-ATPase, 9; Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9-PSMC6-PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process (223 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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