• Version:
  • 11.0 [archived version]
STRINGSTRING
TPM4 TPM4 TPM1 TPM1 TPM2 TPM2 TPM3 TPM3 MYL6B MYL6B DICER1 DICER1 HBG1 HBG1 HBA2 HBA2 HBE1 HBE1 FARSB FARSB HBA1 HBA1 HBG2 HBG2 KNG1 KNG1 CTSL CTSL PSMC3 PSMC3 CTSK CTSK AACT AACT HLA-DPB1 HLA-DPB1 PSMD4 PSMD4 PSMD1 PSMD1 CTSV CTSV GIG25 GIG25 CTSF CTSF CSTA CSTA CNEP1R1 CNEP1R1 SSR4 SSR4
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:
HBA2Hemoglobin subunit alpha 2; Involved in oxygen transport from the lung to the various peripheral tissues; Hemoglobin subunits (142 aa)
CSTACystatin-A; This is an intracellular thiol proteinase inhibitor. Has an important role in desmosome-mediated cell-cell adhesion in the lower levels of the epidermis; Belongs to the cystatin family (98 aa)
KNG1Kininogen-1; (1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin- induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects- (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation [...] (644 aa)
CTSKCathepsin K; Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation; Cathepsins (329 aa)
FARSBphenylalanyl-tRNA synthetase beta subunit; Aminoacyl tRNA synthetases, Class II (589 aa)
PSMD126S proteasome non-ATPase regulatory subunit 1; Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair; Belongs to the proteasome subunit S1 family (953 aa)
CTSFCathepsin F; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins (484 aa)
SSR4Translocon-associated protein subunit delta; TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins; Belongs to the TRAP-delta family (173 aa)
HBA1Hemoglobin subunit alpha; Involved in oxygen transport from the lung to the various peripheral tissues; Belongs to the globin family (142 aa)
HBG1Hemoglobin subunit gamma 1 (147 aa)
TPM4Tropomyosin alpha-4 chain; Tropomyosin 4; Tropomyosins (284 aa)
CTSLCathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins (333 aa)
TPM1Tropomyosin alpha-1 chain; Tropomyosin 1; Tropomyosins (284 aa)
TPM3Tropomyosin alpha-3 chain; Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments; Belongs to the tropomyosin family (285 aa)
PSMD426S proteasome non-ATPase regulatory subunit 4; Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin- [...] (377 aa)
TPM2Tropomyosin beta chain; Tropomyosin 2; Belongs to the tropomyosin family (284 aa)
HBE1Hemoglobin subunit epsilon; The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin; Belongs to the globin family (147 aa)
HBG2Hemoglobin subunit gamma-2; Gamma chains make up the fetal hemoglobin F, in combination with alpha chains; Belongs to the globin family (147 aa)
GIG25Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors (423 aa)
CNEP1R1CTD nuclear envelope phosphatase 1 regulatory subunit 1 (142 aa)
HLA-DPB1HLA class II histocompatibility antigen, DP beta 1 chain; Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for pr [...] (258 aa)
DICER1Endoribonuclease Dicer; Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3’ overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA- induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, a [...] (1922 aa)
CTSVCathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family (334 aa)
MYL6BMyosin light chain 6B; Regulatory light chain of myosin. Does not bind calcium; EF-hand domain containing (208 aa)
AACTAlpha-1-antichymotrypsin; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors (423 aa)
PSMC326S proteasome regulatory subunit 6A; Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC3 belongs to the heterohexameric ring of AAA (ATPases associated wit [...] (439 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
Server load: low (0%) [HD]