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  • 11.0 [archived version]
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PARP15 PARP15 GDAP2 GDAP2 TIPARP TIPARP PARP16 PARP16 PARP11 PARP11 PARP3 PARP3 ZC3HAV1 ZC3HAV1 PARP14 PARP14 PARP9 PARP9 PARP10 PARP10 PARP12 PARP12
"PARP16" - Mono [ADP-ribose] polymerase PARP16 in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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PARP16Mono [ADP-ribose] polymerase PARP16; Intracellular mono-ADP-ribosyltransferase that may play a role in different processes through the mono-ADP-ribosylation of proteins involved in those processes. May play a role in the unfolded protein response (UPR), by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors. May also mediate mono- ADP-ribosylation of karyopherin KPNB1 a nuclear import factor. May not modify proteins on arginine, cysteine or glutamate residues compared to other mono-ADP- ribosyltransferases; Poly(ADP-ribose) polymerases (323 aa)    
Predicted Functional Partners:
PARP3
Poly [ADP-ribose] polymerase 3; Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in t [...] (540 aa)
     
   
  0.798
PARP9
Poly [ADP-ribose] polymerase 9; ADP-ribosyltransferase which, in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses. Within the complex, enhances DTX3L E3 ligase activity which is further enhanced by PARP9 binding to poly(ADP- ribose). In association with DTX3L and in presence of E1 and E2 enzymes, mediates NAD(+)-dependent mono-ADP- ribosylation of ubiquitin which prevents ubiquitin conjugation to substrates such as histones. During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damag [...] (854 aa)
           
  0.736
PARP14
Poly [ADP-ribose] polymerase 14; ADP-ribosyltransferase. By mono-ADP-ribosylating STAT1 at ’Glu-657’ and ’Glu-705’ and thus decreasing STAT1 phosphorylation, negatively regulates pro-inflammatory cytokines production in macrophages in response to IFNG stimulation. Mono-ADP- ribosylates STAT6 (By similarity). Enhances STAT6-dependent transcription (By similarity). In macrophages, positively regulates MRC1 expression in response to IL4 stimulation by promoting STAT6 phosphorylation. Mono-ADP- ribosylates PARP9; Poly(ADP-ribose) polymerases (1801 aa)
           
  0.724
PARP15
Poly [ADP-ribose] polymerase 15; Possesses ADP-ribosyltransferase activity. Transcriptional repressor; Poly(ADP-ribose) polymerases (678 aa)
           
  0.724
PARP10
Poly [ADP-ribose] polymerase 10; May play a role in cell proliferation. May be required for the maintenance of cell cycle progression; Poly(ADP-ribose) polymerases (1025 aa)
     
   
  0.718
GDAP2
Ganglioside induced differentiation associated protein 2; Belongs to the GDAP2 family (497 aa)
           
  0.716
PARP12
poly(ADP-ribose) polymerase family member 12 (701 aa)
           
  0.715
PARP11
Poly [ADP-ribose] polymerase 11; Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (By similarity). In vitro, exhibits mono(ADP-ribosyl) transferase activity; Poly(ADP-ribose) polymerases (338 aa)
           
  0.692
TIPARP
TCDD-inducible poly [ADP-ribose] polymerase; Poly [ADP-ribose] polymerase using NAD(+) as a substrate to transfer ADP-ribose onto glutamic acid residues of a protein acceptor; repeated rounds of ADP-ribosylation leads to the formation of poly(ADPribose) chains on the protein, thereby altering the function of the target protein. May play a role in the adaptive response to chemical exposure (TCDD) and thereby mediates certain effects of the chemicals (By similarity); Poly(ADP-ribose) polymerases (657 aa)
           
  0.692
ZC3HAV1
Zinc finger CCCH-type antiviral protein 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 t [...] (902 aa)
           
  0.688
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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