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 nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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 | VPS18 | vacuolar protein sorting 18 homolog (S. cerevisiae); May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes (973 aa) | ||
 | OAS3 | 2’-5’-oligoadenylate synthetase 3, 100kDa; Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2’-5’- oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in [...] (1087 aa) | ||
 | ORC2 | origin recognition complex, subunit 2; Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (577 aa) | ||
 | OASL | 2’-5’-oligoadenylate synthetase-like; Does not have 2’-5’-OAS activity, but can bind double- stranded RNA. Displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L (514 aa) | ||
 | HUS1 | HUS1 checkpoint homolog (S. pombe); Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3’-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavag [...] (280 aa) | ||
 | ORC4 | origin recognition complex, subunit 4; Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (436 aa) | ||
 | ORC5 | origin recognition complex, subunit 5; Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (435 aa) | ||
 | UBB | ubiquitin B (229 aa) | ||
 | ENSG00000173727 | Uncharacterized protein (112 aa) | ||
 | CALR | calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity) (417 aa) | ||
 | MDH2 | malate dehydrogenase 2, NAD (mitochondrial) (338 aa) | ||
 | UBL4B | ubiquitin-like 4B (174 aa) | ||
 | ZFAND4 | zinc finger, AN1-type domain 4 (727 aa) | ||
 | OAS2 | 2’-5’-oligoadenylate synthetase 2, 69/71kDa; Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2’-5’-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the [...] (719 aa) | ||
 | UBC | ubiquitin C (685 aa) | ||
 | UBL4A | ubiquitin-like 4A; Component of the BAT3 complex, a multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. The complex acts by facilitating TA proteins capture by ASNA1/TRC40- it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins, and transfers them to ASNA1/TRC40 for targeting (157 aa) | ||
 | ORC1 | origin recognition complex, subunit 1; Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (861 aa) | ||
 | HLA-C | major histocompatibility complex, class I, C; Involved in the presentation of foreign antigens to the immune system (By similarity) (366 aa) | ||
 | HLA-A | major histocompatibility complex, class I, A; Involved in the presentation of foreign antigens to the immune system (By similarity) (365 aa) | ||
 | UBD | ubiquitin D (165 aa) | ||
 | ISG15 | ISG15 ubiquitin-like modifier; Ubiquitin-like protein that is conjugated to intracellular target proteins after IFN-alpha or IFN-beta stimulation. Its enzymatic pathway is partially distinct from that of ubiquitin, differing in substrate specificity and interaction with ligating enzymes. ISG15 conjugation pathway uses a dedicated E1 enzyme, but seems to converge with the Ub conjugation pathway at the level of a specific E2 enzyme. Targets include STAT1, SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, EIF2AK2/PKR, MX1/MxA, and RIG-1. Deconjugated by USP18/UBP43. Shows specific chemotactic act [...] (165 aa) | ||
 | OAS1 | 2’-5’-oligoadenylate synthetase 1, 40/46kDa (414 aa) | ||
 | HLA-B | major histocompatibility complex, class I, B; Involved in the presentation of foreign antigens to the immune system (By similarity) (362 aa) | ||
 | ERAP2 | endoplasmic reticulum aminopeptidase 2; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys (960 aa) | ||
 | FAU | Finkel-Biskis-Reilly murine sarcoma virus (FBR-MuSV) ubiquitously expressed (133 aa) | ||
 | B2M | beta-2-microglobulin; Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system (By similarity) (119 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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