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SIRT3 SIRT3 HCCS HCCS HMOX1 HMOX1 COX10 COX10 C7orf55 C7orf55 HEPH HEPH HMOX2 HMOX2 PGRMC1 PGRMC1 CP CP CYP1A2 CYP1A2 PPOX PPOX ABCB7 ABCB7 TIMP2 TIMP2 FECH FECH CETN3 CETN3 NELFB NELFB TRIM74 TRIM74 NELFE NELFE NELFCD NELFCD CETN1 CETN1 PPP2CA PPP2CA PPP2R1A PPP2R1A CETN2 CETN2 EPX EPX PPP2CB PPP2CB CALM3 CALM3
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.
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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
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textmining
co-expression
protein homology
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HMOX1Heme oxygenase 1; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis (288 aa)
PGRMC1Membrane-associated progesterone receptor component 1; Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs); Belongs to the cytochrome b5 family. MAPR subfamily (195 aa)
PPP2CBSerine/threonine-protein phosphatase 2A catalytic subunit beta isoform; PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase; Protein phosphatase catalytic subunits (309 aa)
EPXEosinophil peroxidase; Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis; Belongs to the peroxidase family. XPO subfamily (715 aa)
ABCB7ATP-binding cassette sub-family B member 7, mitochondrial; Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins; ATP binding cassette subfamily B (753 aa)
COX10Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O; Mitochondrial respiratory chain complex assembly factors (443 aa)
TIMP2Metalloproteinase inhibitor 2; Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19; Belongs to the protease inhibitor I35 (TIMP) family (220 aa)
CPCeruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity) (1065 aa)
TRIM74Tripartite motif containing 74; Belongs to the TRIM/RBCC family (250 aa)
CALM3Calmodulin 3 (phosphorylase kinase, delta); Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2 (149 aa)
C7orf55Protein FMC1 homolog; Chromosome 7 open reading frame 55 (113 aa)
CETN1Centrin-1; Plays a fundamental role in microtubule-organizing center structure and function; EF-hand domain containing (172 aa)
PPP2R1ASerine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform; The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT. Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (589 aa)
HCCSCytochrome c-type heme lyase; Links covalently the heme group to the apoprotein of cytochrome c (268 aa)
NELFBNegative elongation factor B; Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. Binds RNA which may help to stabilize the NELF complex on nucleic acid. In vitro, binds weakly to the HIV-1 TAR RNA which is located in the long terminal repeat (LT [...] (580 aa)
CYP1A2Cytochrome P450 1A2; Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen. Participates in the bioactivation of carcinogenic aromatic and heterocyclic amines. Catalizes [...] (516 aa)
PPOXProtoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX (477 aa)
CETN2Centrin-2; Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110; Belongs to the centrin family (172 aa)
NELFENegative elongation factor E; Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. Provides the strongest RNA binding activity of the NELF complex and may initially recruit the NELF complex to RNA. Binds to the HIV-1 TAR RNA which is located in th [...] (380 aa)
SIRT3NAD-dependent protein deacetylase sirtuin-3, mitochondrial; NAD-dependent protein deacetylase. Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues. Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5O. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels; Sirtuins (399 aa)
FECHFerrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family (429 aa)
PPP2CASerine/threonine-protein phosphatase 2A catalytic subunit alpha isoform; PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at ’Ser-259’; Belongs to the PPP phosphatase family. PP-1 subfamily (309 aa)
CETN3Centrin-3; EF-hand domain containing (191 aa)
HEPHHephaestin; May function as a ferroxidase for ferrous (II) to ferric ion (III) conversion and may be involved in copper transport and homeostasis. Implicated in iron homeostasis and may mediate iron efflux associated to ferroportin 1 (1212 aa)
NELFCDNegative elongation factor C/D; Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. Binds RNA which may help to stabilize the NELF complex on nucleic acid. In vitro, the NELFA-NELFCD subcomplex binds to ssDNA and ssRNA in a sequence- and structur [...] (599 aa)
HMOX2Heme oxygenase 2; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter (370 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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