• Version:
  • 11.0 [archived version]
STRINGSTRING
C4orf27 C4orf27 PARP1 PARP1 SMARCB1 SMARCB1 TERF2 TERF2 HMGN4 HMGN4 TERF2IP TERF2IP
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 Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
TERF2Telomeric repeat-binding factor 2; Binds the telomeric double-stranded 5’-TTAGGG-3’ repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5’-TTAGGG-3’ repeats added b [...] (542 aa)
SMARCB1SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1; Core component of the BAF (hSWI/SNF) complex. This ATP- dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric struct [...] (385 aa)
TERF2IPTelomeric repeat-binding factor 2-interacting protein 1; Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HD [...] (399 aa)
PARP1Poly [ADP-ribose] polymerase 1; 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. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T [...] (1014 aa)
HMGN4High mobility group nucleosomal binding domain 4; Belongs to the HMGN family (90 aa)
C4orf27Histone PARylation factor 1; Acts as a cofactor for serine ADP-ribosylation by conferring serine specificity on PARP1 and PARP2- interacts with PARP1 and PARP1 and is able to change amino acid specificity toward serine. Promotes histone serine ADP- ribosylation in response to DNA damage, limiting DNA damage- induced PARP1 hyper-automodification, and ensuring genome stability (346 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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