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STRINGSTRING
HIST1H2BJ HIST1H2BJ HIST1H2BM HIST1H2BM LEPRE1 LEPRE1 FUBP3 FUBP3 RPL39L RPL39L CALU CALU WDR4 WDR4 CIAO1 CIAO1 UBC UBC RPL39 RPL39 ELAVL1 ELAVL1 SRP9 SRP9 SRP14 SRP14 AARS AARS UBXN7 UBXN7 DHPS DHPS CD44 CD44 PFDN1 PFDN1 DPP8 DPP8 PRND PRND ARMC9 ARMC9 CXCL10 CXCL10 CXCL11 CXCL11
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
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:
DHPSdeoxyhypusine synthase; Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue (369 aa)
ARMC9armadillo repeat containing 9 (665 aa)
AARSalanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain (By similarity) (968 aa)
PFDN1prefoldin subunit 1; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (122 aa)
SRP14signal recognition particle 14kDa (homologous Alu RNA binding protein); Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (136 aa)
RPL39Lribosomal protein L39-like (51 aa)
UBXN7UBX domain protein 7 (489 aa)
LEPRE1leucine proline-enriched proteoglycan (leprecan) 1 (736 aa)
SRP9signal recognition particle 9kDa; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (86 aa)
CXCL10chemokine (C-X-C motif) ligand 10; Chemotactic for monocytes and T-lymphocytes. Binds to CXCR3 (98 aa)
CXCL11chemokine (C-X-C motif) ligand 11; Chemotactic for interleukin-activated T-cells but not unstimulated T-cells, neutrophils or monocytes. Induces calcium release in activated T-cells. Binds to CXCR3. May play an important role in CNS diseases which involve T-cell recruitment. May play a role in skin immune responses (94 aa)
PRNDprion protein 2 (dublet) (176 aa)
FUBP3far upstream element (FUSE) binding protein 3; May interact with single-stranded DNA from the far- upstream element (FUSE). May activate gene expression (572 aa)
WDR4WD repeat domain 4; Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational change of the catalytic subunit (412 aa)
DPP8dipeptidyl-peptidase 8 (898 aa)
HIST1H2BJhistone cluster 1, H2bj; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (126 aa)
UBCubiquitin C (685 aa)
HIST1H2BMhistone cluster 1, H2bm; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity) (126 aa)
RPL39ribosomal protein L39 (51 aa)
ELAVL1ELAV (embryonic lethal, abnormal vision, Drosophila)-like 1 (Hu antigen R); Involved in 3’-UTR ARE-mediated MYC stabilization. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, HUR binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA and AUUUUUA motifs. Binds preferentially to the 5’-UUUU[AG]UUU-3’ motif in vitro (326 aa)
CD44CD44 molecule (Indian blood group) (742 aa)
CIAO1cytosolic iron-sulfur protein assembly 1; Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to specifically modulate the transactivation activity of WT1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (339 aa)
CALUcalumenin (323 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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