TRIM48 protein (Homo sapiens) - STRING network view

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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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protein of unknown 3D structure

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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

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Predicted Interactions

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Score

TRIM48

tripartite motif containing 48 (224 aa)

Predicted Functional Partners:

UBC

0.433

SSRP1

0.405

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man

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structured XML interaction data, according to the 'PSI-MI' data standard

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... protein sequences:

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MFA: multi-fasta format - containing the aminoacid sequences in the network

... protein annotations:

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a tab-delimited file describing the names, domains and annotated functions of the network proteins

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
SSRP1	TRIM48	ENSP00000278412	ENSP00000402414	structure specific recognition protein 1; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the ree [...]	tripartite motif containing 48	0.405
SSRP1	UBC	ENSP00000278412	ENSP00000344818	structure specific recognition protein 1; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the ree [...]	ubiquitin C	0.952
TRIM48	SSRP1	ENSP00000402414	ENSP00000278412	tripartite motif containing 48	structure specific recognition protein 1; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the ree [...]	0.405
TRIM48	UBC	ENSP00000402414	ENSP00000344818	tripartite motif containing 48	ubiquitin C	0.433
UBC	SSRP1	ENSP00000344818	ENSP00000278412	ubiquitin C	structure specific recognition protein 1; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the ree [...]	0.952
UBC	TRIM48	ENSP00000344818	ENSP00000402414	ubiquitin C	tripartite motif containing 48	0.433

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