CSF1R

Homo sapiens (Human)

Proto-oncogene c-Fms; M-CSF-R; FMS; CSF-1R; CSF-1-R; CSF-1 receptor; CD115

Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily

Kinase

Promotes the release of proinflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor. Tyrosine-protein kinase that acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes.

Aberrant expression of CSF1 or CSF1R can promote cancer cell proliferation, invasion and formation of metastases. Overexpression of CSF1 or CSF1R is observed in a significant percentage of breast, ovarian, prostate, and endometrial cancers.; DISEASE: Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.; DISEASE: Leukoencephalopathy, hereditary diffuse, with spheroids 1 (HDLS1) [MIM:221820]: An autosomal dominant adult-onset rapidly progressive neurodegenerative disorder characterized by variable behavioral, cognitive, and motor changes. Patients often die of dementia within 6 years of onset. Brain imaging shows patchy abnormalities in the cerebral white matter, predominantly affecting the frontal and parietal lobes. {ECO:0000269|PubMed:22197934, ECO:0000269|PubMed:23408870, ECO:0000269|PubMed:24336230, ECO:0000269|PubMed:24532199}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Brain abnormalities, neurodegeneration, and dysosteosclerosis (BANDDOS) [MIM:618476]: An autosomal recessive disease with variable manifestations. Main features are brain malformations with calcifying leukoencephalopathy, progressive neurodegeneration, and bone sclerotic features. The age at onset ranges from infancy to early adulthood. Neurologic features include loss of previous motor and language skills, cognitive impairment, spasticity, and focal seizures. Brain imaging shows periventricular white matter abnormalities and calcifications, large cisterna magna or Dandy-Walker malformation, and sometimes agenesis of the corpus callosum. {ECO:0000269|PubMed:30982608, ECO:0000269|PubMed:30982609}. The disease is caused by variants affecting the gene represented in this entry.

DB07167; DB07202; DB12147; DB12010; DB00619; DB06080; DB12978; DB01268

P09603; Q15375; P29323; Q6ZMJ4-1

EC 2.7.10.1

3D-structure; Alternative splicing; ATP-binding; Cell membrane; Disease variant; Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Inflammatory response; Innate immunity; Kinase; Membrane; Neurodegeneration; Nucleotide-binding; Phosphoprotein; Proteomics identification; Proto-oncogene; Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation

A

35082.9

311

0.11

44.6

8.13

2.42

-8.89

MAOA

Homo sapiens (Human)

Monoamine oxidase A; Amine oxidase [flavin-containing] A

Flavin monoamine oxidase family

CH-NH(2) donor oxidoreductase

MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine. Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues.

Brunner syndrome (BRNRS) [MIM:300615]: A form of X-linked non-dysmorphic mild intellectual disability. Male patients are affected by borderline intellectual deficit and exhibit abnormal behavior, including disturbed regulation of impulsive aggression. Obligate female carriers have normal intelligence and behavior. {ECO:0000269|PubMed:8211186}. The disease is caused by variants affecting the gene represented in this entry.

DB01472; DB00918; DB00182; DB06698; DB04889; DB13876; DB01445; DB06774; DB00215; DB04017; DB09130; DB05205; DB07641; DB00988; DB01363; DB00668; DB12329; DB01175; DB03147; DB14914; DB00614; DB01381; DB07919; DB04818; DB01247; DB00601; DB01577; DB00805; DB01442; DB01171; DB08804; DB00952; DB04820; DB00184; DB04821; DB06412; DB01626; DB00780; DB00191; DB00388; DB00397; DB09244; DB04850; DB00721; DB01168; DB00571; DB00852; DB09363; DB00140; DB00953; DB06654; DB01037; DB01104; DB00669; DB14569; DB09042; DB00624; DB13943; DB13944; DB13946; DB09245; DB00752; DB15328; DB09185; DB04832; DB00315; DB00909

P27338

EC 1.4.3.4

3D-structure; Acetylation; Alternative splicing; Catecholamine metabolism; Direct protein sequencing; Disease variant; FAD; Flavoprotein; Intellectual disability; Membrane; Mitochondrion; Mitochondrion outer membrane; Neurotransmitter degradation; Oxidoreductase; Phosphoprotein; Proteomics identification; Reference proteome; Transmembrane; Transmembrane helix

A

58195.3

513

0.11

34.97

7.98

2.87

-8.89

AKR1C3

Homo sapiens (Human)

NA

PGFS;DDH1;HSD17B5;KIAA0119

Aldo/keto reductase family

Oxidoreductase

15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity.Alditol:NADP+ 1-oxidoreductase activity.Aldo-keto reductase (NADP) activity.Androsterone dehydrogenase activity.Delta4-3-oxosteroid 5beta-reductase activity.Dihydrotestosterone 17-beta-dehydrogenase activity.Geranylgeranyl reductase activity.Indanol dehydrogenase activity.Ketoreductase activity.Ketosteroid monooxygenase activity.NADP-retinol dehydrogenase activity.Oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor.Phenanthrene 9,10-monooxygenase activity.Prostaglandin D2 11-ketoreductase activity.Prostaglandin-F synthase activity.Prostaglandin H2 endoperoxidase reductase activity.Retinal dehydrogenase activity.Retinol dehydrogenase activity.Testosterone 17-beta-dehydrogenase (NADP+) activity.Testosterone dehydrogenase (NAD+) activity.Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity.

Neurodevelopmental disorder with language impairment and behavioral abnormalities (NEDLIB) [MIM:618917]: A neurodevelopmental disorder characterized by global developmental delay, impaired intellectual development, poor or absent speech, and behavioral abnormalities, such as autism spectrum disorder, repetitive behaviors, and hyperactivity. Some patients develop seizures and manifest developmental regression. {ECO:0000269|PubMed:31300657}. The disease is caused by variants affecting the gene represented in this entry. The genetic variation producing the missense variant p.Q607E, associated with NEDLIB, is predicted to deeply affect RNA editing. In a physiological context, the adenosine (A) residue of the original glutamine (Q) codon CAG is post-transcriptionaly edited to inosine (I) by ADAR2, leading to a codon recognized by the ribosome as arginine (R). The glutamate (E) codon GAG, resulting from the genetic variation, is predicted to be edited 90% less than the normal CAG codon. If edited, the codon GIG would be translated as p.Q607G. {ECO:0000305|PubMed:31300657}.

DB07700; DB01561; DB01536; DB00997; DB01039; DB02266; DB13751; DB00328; DB06077; DB00959; DB00157; DB03461; DB09074; DB00776; DB02056; DB01698; DB02901

P17516

1.1.1.-; 1.1.1.188; 1.1.1.210; 1.1.1.239; 1.1.1.357; 1.1.1.53; 1.1.1.62; 1.1.1.64

3D-structure; Alternative splicing; Cytoplasm; Lipid metabolism; NAD; NADP; Oxidoreductase; Proteomics identification; Reference proteome

A

35846.8

315

0.09

47.59

8.54

4.51

-8.89

fccA

Shewanella frigidimarina

NA

fcc3

FAD-dependent oxidoreductase 2 family, FRD/SDH subfamily

Oxidoreductase

Electron carrier activity.Fumarate reductase (menaquinone).Metal ion binding.Nucleic acid binding.Succinate dehydrogenase activity.

Pigmentary disorder, reticulate, with systemic manifestations, X-linked (PDR) [MIM:301220]: An X-linked recessive disorder characterized by recurrent infections and sterile inflammation in various organs. Diffuse skin hyperpigmentation with a distinctive reticulate pattern is universally evident by early childhood. This is later followed in many patients by hypohidrosis, corneal inflammation and scarring, enterocolitis that resembles inflammatory bowel disease, and recurrent urethral strictures. Melanin and amyloid deposition is present in the dermis. Affected males also have a characteristic facies with frontally upswept hair and flared eyebrows. Female carriers have only restricted pigmentary changes along Blaschko's lines. {ECO:0000269|PubMed:27019227}. The disease is caused by variants affecting the gene represented in this entry. XLPDR is caused by a recurrent intronic mutation that results in missplicing and reduced POLA1 expression. This leads to a decrease in cytosolic RNA:DNA hybrids and constitutive activation of type I interferon responses, but has no effect on cell replication. {ECO:0000269|PubMed:27019227}.; DISEASE: Van Esch-O'Driscoll syndrome (VEODS) [MIM:301030]: An X-linked recessive syndrome characterized by different degrees of intellectual disability, moderate to severe short stature, microcephaly, hypogonadism, and variable congenital malformations. {ECO:0000269|PubMed:31006512}. The disease is caused by variants affecting the gene represented in this entry.

DB04734; DB03147; DB01677; DB03343

NA

1.3.2.4

3D-structure; Electron transport; FAD; Flavoprotein; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Transport

A

60177.2

568

0.06

27.7

6

-8.64

-8.88

fabF

Escherichia coli (strain K12)

NA

JW1081;b1095;fabJ

Thiolase-like superfamily, Beta-ketoacyl-ACP synthases family

Transferase

3-oxoacyl-[acyl-carrier-protein] synthase activity.Beta-ketoacyl-acyl-carrier-protein synthase II activity.

Pigmentary disorder, reticulate, with systemic manifestations, X-linked (PDR) [MIM:301220]: An X-linked recessive disorder characterized by recurrent infections and sterile inflammation in various organs. Diffuse skin hyperpigmentation with a distinctive reticulate pattern is universally evident by early childhood. This is later followed in many patients by hypohidrosis, corneal inflammation and scarring, enterocolitis that resembles inflammatory bowel disease, and recurrent urethral strictures. Melanin and amyloid deposition is present in the dermis. Affected males also have a characteristic facies with frontally upswept hair and flared eyebrows. Female carriers have only restricted pigmentary changes along Blaschko's lines. {ECO:0000269|PubMed:27019227}. The disease is caused by variants affecting the gene represented in this entry. XLPDR is caused by a recurrent intronic mutation that results in missplicing and reduced POLA1 expression. This leads to a decrease in cytosolic RNA:DNA hybrids and constitutive activation of type I interferon responses, but has no effect on cell replication. {ECO:0000269|PubMed:27019227}.; DISEASE: Van Esch-O'Driscoll syndrome (VEODS) [MIM:301030]: An X-linked recessive syndrome characterized by different degrees of intellectual disability, moderate to severe short stature, microcephaly, hypogonadism, and variable congenital malformations. {ECO:0000269|PubMed:31006512}. The disease is caused by variants affecting the gene represented in this entry.

DB08366; DB01034; DB03017; DB08407

P0A6Y8

2.3.1.179

3D-structure; Acyltransferase; Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase

A

42794.9

411

0.06

31.41

5.72

-7.34

-8.88

GRIN2A

Homo sapiens (Human)

NR2A; NMDA receptor NR2A; N-methyl D-aspartate receptor subtype 2A; HNR2A; Glutamate receptor ionotropic, NMDA 2A; Glutamate [NMDA] receptor subunit epsilon-1; GluN2A

Glutamate-gated ion channel (TC 1.A.10.1) family, NR1/GRIN1 subfamily

Glutamate-gated ion channel

Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition; channels containing GRIN1 and GRIN2A have higher sensitivity to glutamate and faster kinetics than channels formed by GRIN1 and GRIN2B. Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning. Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium.

Neurodevelopmental disorder with or without hyperkinetic movements and seizures, autosomal dominant (NDHMSD) [MIM:614254]: An autosomal dominant neurodevelopmental disorder characterized by severe intellectual disability and developmental delay, absent speech, muscular hypotonia, dyskinesia, and hyperkinetic movements. Cortical blindness, cerebral atrophy, and seizures are present in some patients. {ECO:0000269|PubMed:21376300, ECO:0000269|PubMed:25167861, ECO:0000269|PubMed:25864721, ECO:0000269|PubMed:27164704, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:28228639, ECO:0000269|PubMed:28389307, ECO:0000269|PubMed:38538865}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neurodevelopmental disorder with or without hyperkinetic movements and seizures, autosomal recessive (NDHMSR) [MIM:617820]: An autosomal recessive neurodevelopmental disorder characterized by severe intellectual disability and psychomotor developmental delay, involuntary and stereotypic movements, spasticity, and inability to walk without support. Intractable seizures manifest in some patients. {ECO:0000269|PubMed:27164704, ECO:0000269|PubMed:28051072}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental and epileptic encephalopathy 101 (DEE101) [MIM:619814]: A form of epileptic encephalopathy, a heterogeneous group of early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE101 is an autosomal recessive, severe form characterized by onset of seizures in early infancy. Death in infancy may occur. {ECO:0000269|PubMed:27164704, ECO:0000269|PubMed:34611970}. The disease is caused by variants affecting the gene represented in this entry.

DB01931; DB00659; DB06151; DB08838; DB01238; DB00289; DB05824; DB04620; DB03929; DB00647; DB00843; DB00228; DB11823; DB13146; DB06741; DB00142; DB00874; DB08954; DB06738; DB09409; DB09481; DB01043; DB00454; DB00333; DB04896; DB01173; DB00312; DB01174; DB01708; DB00418; DB00193

P05067; P35637; Q12879-1; Q13224; Q62936

NA

3D-structure; Alternative splicing; Calcium; Cell membrane; Disease variant; Disulfide bond; Epilepsy; Glycoprotein; Intellectual disability; Ion channel; Ion transport; Ligand-gated ion channel; Magnesium; Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane; Proteomics identification; Receptor; Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix; Transport; Zinc

B

63184.8

559

0.1

29.67

8.51

6.66

-8.87

MTNR1A

Homo sapiens (Human)

Mel1a receptor; Mel1AR; Mel-1A-R

G-protein coupled receptor 1 family

GPCR rhodopsin

Likely to mediate the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity. High affinity receptor for melatonin.

Spermatogenic failure 5 (SPGF5) [MIM:243060]: An infertility disorder caused by spermatogenesis defects. Semen from affected men show close to 100% morphologically abnormal multiflagellar spermatozoa with low motility, oversized irregular heads, and abnormal midpiece and acrosome. {ECO:0000269|PubMed:17435757, ECO:0000269|PubMed:21733974}. The disease is caused by variants affecting the gene represented in this entry.

DB06594; DB01065; DB00980; DB02709; DB09071

P27797; A8MQ03; Q8IUG1; P49286; O76081; P57088

NA

3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; Receptor; Reference proteome; Transducer; Transmembrane; Transmembrane helix

D

31301

276

0.15

37.33

9.22

9.92

-8.88

ache

Tetronarce californica (Pacific electric ray) (Torpedo californica)

NA

NA

Type-B carboxylesterase/lipase family

NA

Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.

Noonan syndrome 5 (NS5) [MIM:611553]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. {ECO:0000269|PubMed:17603482, ECO:0000269|PubMed:17603483, ECO:0000269|PubMed:20683980}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: LEOPARD syndrome 2 (LPRD2) [MIM:611554]: A disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness. {ECO:0000269|PubMed:17603483}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated, 1NN (CMD1NN) [MIM:615916]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:24777450}. The disease is caused by variants affecting the gene represented in this entry.

NA

NA

3.1.1.7

3D-structure; Alternative splicing; Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation; Serine esterase; Signal; Synapse

A

59779.2

529

0.12

48.49

5.8

-8.48

-8.86

NOS3

Homo sapiens (Human)

Nitric oxide synthase, endothelial; NOSIII; NOS,type III; NOS type III; Endothelial nitric oxide synthase; Endothelial NOS; ENOS; EC-NOS; Constitutive NOS; CNOS

NOS family

Paired donor oxygen oxidoreductase

NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets. Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway.

Variation Asp-298 in NOS3 may be associated with susceptibility to coronary spasm. {ECO:0000269|PubMed:11740345, ECO:0000269|PubMed:9737779}.

DB07001; DB02048; DB02911; DB02335; DB01997; DB03332; DB04534; DB07244; DB03100; DB03918; DB02207; DB03065; DB00125; DB02994; DB01833; DB00155; DB00997; DB07388; DB03974; DB02077; DB01821; DB09237; DB01110; DB03144; DB03305; DB01686; DB04559; DB02044; DB08019; DB08018; DB02027; DB02979; DB00435; DB04223; DB06154; DB03910; DB02141; DB03963; DB03707; DB02234; DB04018; DB00360; DB02589

P60709; P63010-2; Q8N6T3-3; Q9Y575-3; Q96FT7-4; Q5SZD1; Q16543; Q9UNS2; Q8IUI8; P35222; Q05193; O15287; Q08379; Q71DI3; P69905; P61978; Q12891; Q9UKT9; Q9Y2M5; Q14525; Q6DKI2; P43364-2; Q8N6F8; O94851; A4FUJ8; Q8N594; Q8IVI9; Q6X4W1-6; O15381-5; Q9NV79; Q16549; Q5T2W1; O75925; Q96I34; Q6ZMI0-5; P57052; Q9GZR2; Q96D59; Q8N6K7-2; Q9GZS3; Q8IUW3; Q7Z699; Q7Z698; P50502; Q9BR01-2; Q9NVV9; Q86WT6-2; Q9H347; P58304; Q9NZC7-5; Q9UNY5; P14079

EC 1.14.13.39

3D-structure; Alternative splicing; Calcium; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing; FAD; Flavoprotein; FMN; Golgi apparatus; Heme; Iron; Lipoprotein; Membrane; Metal-binding; Myristate; NADP; Oxidoreductase; Palmitate; Phosphoprotein; Proteomics identification; Reference proteome; Zinc

A,B

90790.1

803

0.11

50.67

6.03

-9.56

-8.87

MTNR1B

Homo sapiens (Human)

Mel1b receptor; Mel1b melatonin receptor; Mel-1B-R

G-protein coupled receptor 1 family

GPCR rhodopsin

Likely to mediate the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity. High affinity receptor for melatonin.

Insulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]: A disorder characterized by intrauterine growth retardation, poor postnatal growth and increased plasma IGF1 levels. {ECO:0000269|PubMed:14657428, ECO:0000269|PubMed:15928254, ECO:0000269|PubMed:25040157}. The disease is caused by variants affecting the gene represented in this entry.

DB06594; DB01065; DB00980; DB02709; DB09071; DB15133

P28335; P48039; O76081; Q14669

NA

3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; Receptor; Reference proteome; Transducer; Transmembrane; Transmembrane helix

A

50184.9

448

0.11

37.2

5.72

-5.68

-8.87

PTGDR2

Homo sapiens (Human)

PTGDR2; Chemoattractant receptor-homologous molecule expressed on Th2 cells; CD294

G-protein coupled receptor 1 family

GPCR rhodopsin

Receptor for prostaglandin D2 (PGD2). Coupled to the G(i)-protein. Receptor activation may result in pertussis toxin- sensitive decreases in cAMP levels and Ca(2+) mobilization. PI3K signaling is also implicated in mediating PTGDR2 effects. PGD2 induced receptor internalization. CRTH2 internalization can be regulated by diverse kinases such as, PKC, PKA, ADRBK1/GRK2, GPRK5/GRK5 and GRK6. Receptoractivation is responsible, at least in part, in immune regulation and allergic/inflammation responses.

Neurodevelopmental disorder with seizures, hypotonia, and brain imaging abnormalities (NEDSHBA) [MIM:618922]: An autosomal recessive neurodevelopmental disorder characterized by global developmental delay, hypotonia, severe to profound intellectual disability, early-onset epilepsy, and microcephaly. Neuroimaging shows cerebral atrophy, thin corpus callosum and hypomyelination in a majority of cases. Death in childhood may occur. {ECO:0000269|PubMed:27435318, ECO:0000269|PubMed:28097321, ECO:0000269|PubMed:32286009, ECO:0000269|PubMed:33476302, ECO:0000269|PubMed:33500274}. The disease is caused by variants affecting the gene represented in this entry.

DB00770; DB12789; DB00917; DB01088; DB00328; DB02056; DB13036; DB00605; DB04828

NA

NA

3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; Proteomics identification; Receptor; Reference proteome; Transducer; Transmembrane; Transmembrane helix

A

49740.6

447

0.1

37.89

10.13

21.88

-8.86

GOT1

Homo sapiens (Human)

Glutamate oxaloacetate transaminase-1; GOT1

Class-I pyridoxal-phosphate-dependent aminotransferase family

Transaminase

Biosynthesis of L-glutamate from L-aspartate or L- cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3- mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain.

Multiple fibroadenomas of the breast (MFAB) [MIM:615554]: A benign breast disease marked by lobuloalveolar growth with abnormally high proliferation of the epithelium, and characterized by the presence of more than 3 fibroadenomas in one breast. Fibroadenomas are adenomas containing fibrous tissue. {ECO:0000269|PubMed:18779591}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hyperprolactinemia (HPRL) [MIM:615555]: A disorder characterized by increased levels of prolactin in the blood not associated with gestation or the puerperium. HPRL may result in infertility, hypogonadism, and galactorrhea. {ECO:0000269|PubMed:24195502}. The disease is caused by variants affecting the gene represented in this entry.

DB00210; DB00128; DB09130; DB00151; DB00142; DB04299; DB00114

NA

EC 2.6.1.1

3D-structure; Alternative splicing; Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Direct protein sequencing; Phosphoprotein; Proteomics identification; Pyridoxal phosphate; Reference proteome; Transferase

A,B,C,D

51732.3

462

0.1

31.83

7.48

0.86

-8.85

DHODH

Homo sapiens (Human)

Dihydroorotate oxidase; Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOdehase; DHODH

Dihydroorotate dehydrogenase family, Type 2 subfamily

CH-CH donor oxidoreductase

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

Postaxial acrofacial dysostosis (POADS) [MIM:263750]: POADS is characterized by severe micrognathia, cleft lip and/or palate, hypoplasia or aplasia of the posterior elements of the limbs, coloboma of the eyelids and supernumerary nipples. POADS is a very rare disorder: only 2 multiplex families, each consisting of 2 affected siblings born to unaffected, nonconsanguineous parents, have been described among a total of around 30 reported cases. {ECO:0000269|PubMed:19915526}. The disease is caused by variants affecting the gene represented in this entry.

DB07559; DB07561; DB08172; DB08169; DB07443; DB07978; DB07975; DB04281; DB08249; DB07977; DB07976; DB04583; DB08008; DB01117; DB03523; DB03480; DB02613; DB04147; DB03247; DB01097; DB06481; DB08006; DB02262; DB05125; DB08880; DB07646

Q6ZMZ0; P49638

EC 1.3.5.2

3D-structure; Disease variant; Flavoprotein; FMN; Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Proteomics identification; Pyrimidine biosynthesis; Reference proteome; Transit peptide; Transmembrane; Transmembrane helix

A

38341.4

353

0.05

39.27

9.28

5.52

-8.85

CYP3A4

Homo sapiens (Human)

Taurochenodeoxycholate 6-alpha-hydroxylase; Quinine 3-monooxygenase; P450-PCN1; Nifedipine oxidase; NF-25; HLp; Cytochrome P450-PCN1; Cytochrome P450 NF-25; Cytochrome P450 HLp; Cytochrome P450 3A4; C

Cytochrome P450 family

Paired donor oxygen oxidoreductase

In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e. g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4-hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,8-cineole 2-exo-monooxygenase. The enzyme also hydroxylates etoposide. Catalyzes 4-beta-hydroxylation of cholesterol. May catalyze 25-hydroxylation of cholesterol in vitro. Catalyzes sulfoxidation of the anthelmintics albendazole and fenbendazole. Cytochromes P450 are a group of heme-thiolate monooxygenases.

Vitamin D-dependent rickets 3 (VDDR3) [MIM:619073]: An autosomal dominant disorder of vitamin D metabolism resulting in early-onset rickets, reduced serum levels of the vitamin D metabolites 25-hydroxyvitamin D and 1,25-dihydroxyvitamin D, and deficient responsiveness to parent and activated forms of vitamin D. {ECO:0000269|PubMed:29461981}. The gene represented in this entry is involved in disease pathogenesis.

DB08496; DB14055; DB12537; DB12629; DB01456; DB04070; DB11919; DB12515; DB11932; DB12001; DB05812; DB14973; DB11703; DB01418; DB00316; DB00819; DB15568; DB00546; DB08838; DB00518; DB00240; DB00041; DB04630; DB00802; DB00346; DB09026; DB00918; DB06203; DB00969; DB12015; DB14003; DB00404; DB06403; DB06742; DB13141; DB00288; DB00357; DB01424; DB01223; DB01118; DB00321; DB00381; DB00701; DB01217; DB01536; DB01435; DB11901; DB06605; DB00714; DB05676; DB00673; DB01352; DB09229; DB00278; DB01238; DB14185; DB06413; DB01169; DB06697; DB12597; DB06216; DB00637; DB11586; DB01072; DB16098; DB01076; DB01117; DB15011; DB06237; DB15233; DB06442; DB11995; DB06318; DB06626; DB00972; DB09230; DB04957; DB00207; DB12781; DB13997; DB04975; DB01483; DB11817; DB09227; DB00394; DB08903; DB05015; DB16703; DB15463; DB13488; DB09231; DB00865; DB01244; DB15982; DB00443; DB14669; DB12236; DB00307; DB01393; DB01128; DB11799; DB04794; DB00905; DB13746; DB16536; DB00612; DB13975; DB09223; DB08873; DB00188; DB00559; DB06616; DB07348; DB08870; DB09128; DB12267; DB01194; DB05541; DB01200; DB09017; DB11752; DB01222; DB00297; DB00921; DB00490; DB01008; DB09173; DB06772; DB00248; DB08875; DB00201; DB04886; DB00136; DB08907; DB01152; DB09061; DB14737; DB12218; DB11791; DB08502; DB06774; DB00564; DB11383; DB11960; DB06016; DB13835; DB01136; DB14984; DB06634; DB00520; DB01333; DB00482; DB06119; DB09063; DB00439; DB06419; DB00185; DB06777; DB00446; DB00475; DB13528; DB00608; DB00856; DB01114; DB00477; DB00356; DB00169; DB01410; DB09201; DB09232; DB01166; DB00501; DB01012; DB00568; DB00537; DB00604; DB00215; DB01211; DB12499; DB04920; DB01190; DB00349; DB11750; DB01013; DB13158; DB14652; DB00845; DB00636; DB06470; DB01242; DB01068; DB00575; DB00758; DB13843; DB00628; DB01559; DB00257; DB00363; DB09065; DB05239; DB00907; DB00318; DB01394; DB06342; DB00872; DB00286; DB12483; DB04652; DB01285; DB14681; DB01380; DB13003; DB08865; DB11672; DB14635; DB04838; DB00924; DB00531; DB00091; DB04839; DB00987; DB08912; DB09102; DB11963; DB01764; DB01406; DB11779; DB06292; DB04884; DB11682; DB00250; DB15031; DB00496; DB09234; DB12941; DB01264; DB09183; DB01254; DB00694; DB01609; DB11921; DB11943; DB11637; DB00705; DB13857; DB01151; DB00304; DB01260; DB06780; DB01134; DB06700; DB12161; DB01234; DB14649; DB11487; DB09555; DB05351; DB04856; DB14068; DB00514; DB00647; DB14063; DB11994; DB00829; DB00586; DB00485; DB09123; DB00255; DB09095; DB06781; DB01396; DB11274; DB01551; DB11273; DB13345; DB13385; DB00320; DB00343; DB01093; DB08995; DB13347; DB00954; DB00280; DB00822; DB02520; DB01248; DB00204; DB00757; DB08930; DB01184; DB00843; DB11400; DB12301; DB06446; DB05928; DB00590; DB01142; DB00997; DB00254; DB00470; DB04855; DB01395; DB00476; DB11952; DB00378; DB11742; DB14240; DB01127; DB14598; DB14600; DB00625; DB09235; DB06374; DB11979; DB11574; DB00216; DB15444; DB09039; DB09101; DB14064; DB13874; DB11718; DB13007; DB11986; DB08899; DB08992; DB00751; DB00668; DB00700; DB12266; DB01873; DB11405; DB03515; DB02187; DB12329; DB12147; DB01049; DB01253; DB00696; DB00530; DB00199; DB01175; DB11823; DB14575; DB09119; DB00736; DB01215; DB09381; DB12235; DB00783; DB13952; DB13953; DB13954; DB13955; DB13956; DB01196; DB00655; DB04574; DB00402; DB00330; DB00898; DB00977; DB00593; DB08794; DB01466; DB00823; DB09166; DB00294; DB00773; DB01628; DB14766; DB06414; DB13866; DB01590; DB00990; DB00973; DB12500; DB00949; DB01023; DB08980; DB00574; DB00813; DB06702; DB12265; DB08874; DB01216; DB16165; DB13961; DB04908; DB00301; DB00196; DB00687; DB00663; DB04841; DB00180; DB01544; DB00591; DB01047; DB08971; DB00324; DB00472; DB08970; DB14634; DB09378; DB14637; DB00846; DB00690; DB13338; DB04842; DB00499; DB13867; DB08906; DB00588; DB01095; DB00176; DB12307; DB08905; DB01319; DB06717; DB14019; DB01320; DB12010; DB11796; DB11679; DB00947; DB02703; DB15149; DB00674; DB12923; DB05087; DB00317; DB01241; DB01645; DB12184; DB06730; DB11619; DB12141; DB01381; DB11978; DB13879; DB00143; DB01016; DB08909; DB00986; DB05814; DB00889; DB10534; DB11575; DB00365; DB00400; DB01018; DB06786; DB01218; DB13728; DB00502; DB01159; DB05212; DB01275; DB00956; DB00769; DB00741; DB14538; DB14539; DB14540; DB14541; DB14542; DB14543; DB14545; DB14544; DB01611; DB14570; DB06789; DB00557; DB12471; DB09053; DB01050; DB11737; DB09054; DB01181; DB04946; DB00619; DB09262; DB00458; DB00724; DB05039; DB08953; DB00808; DB00224; DB06370; DB11886; DB13293; DB01029; DB00762; DB11633; DB06636; DB00951; DB00982; DB00270; DB11757; DB01167; DB09083; DB08820; DB00602; DB14568; DB04845; DB09570; DB01221; DB01587; DB06738; DB01026; DB09309; DB05903; DB09236; DB06218; DB06791; DB00448; DB01259; DB06685; DB14723; DB12825; DB11951; DB15673; DB16217; DB09078; DB00528; DB11560; DB06469; DB12070; DB01006; DB01227; DB09237; DB01002; DB06282; DB05667; DB00825; DB08918; DB00367; DB00281; DB13766; DB08882; DB17083; DB01583; DB00589; DB09198; DB14065; DB08827; DB01206; DB06448; DB16222; DB00836; DB01601; DB00455; DB00186; DB04871; DB12130; DB09195; DB12089; DB00678; DB14596; DB00227; DB09212; DB08933; DB09280; DB06077; DB06708; DB08815; DB12674; DB12474; DB04829; DB13074; DB08932; DB09238; DB16226; DB04835; DB06234; DB14921; DB00643; DB14009; DB09124; DB00603; DB00253; DB00358; DB00351; DB11529; DB14659; DB00814; DB00170; DB00454; DB09383; DB01071; DB01357; DB04817; DB00333; DB04833; DB00763; DB00563; DB01028; DB09241; DB00353; DB00959; DB14644; DB12952; DB06710; DB00247; DB01233; DB00264; DB00916; DB01011; DB15489; DB00379; DB06148; DB01388; DB01110; DB00683; DB13456; DB06595; DB00834; DB04896; DB13287; DB08893; DB11792; DB00370; DB12489; DB16236; DB06587; DB00648; DB01204; DB16390; DB00745; DB11763; DB00764; DB14512; DB00471; DB00295; DB09205; DB00688; DB01024; DB11605; DB00486; DB14011; DB00607; DB12092; DB11691; DB06230; DB09049; DB01183; DB00731; DB04861; DB01149; DB00220; DB11828; DB09199; DB09048; DB00238; DB00627; DB00622; DB02701; DB00184; DB01115; DB09239; DB04868; DB09240; DB06712; DB04743; DB00393; DB09079; DB16691; DB12005; DB00401; DB01595; DB01054; DB00435; DB11636; DB13981; DB06713; DB14678; DB00717; DB09371; DB01059; DB00957; DB09389; DB00540; DB06174; DB06152; DB00104; DB06670; DB00334; DB09074; DB11442; DB14881; DB00768; DB16267; DB12513; DB09568; DB00338; DB00904; DB11130; DB04911; DB01083; DB01173; DB11837; DB09330; DB04938; DB13500; DB00776; DB12532; DB00239; DB01062; DB00497; DB06412; DB01192; DB12612; DB01229; DB11697; DB09073; DB01267; DB00377; DB05467; DB06603; DB00213; DB00617; DB01384; DB08439; DB00910; DB09297; DB00715; DB06663; DB03010; DB06589; DB00082; DB15102; DB13791; DB00312; DB11198; DB08883; DB01186; DB01074; DB08922; DB00850; DB12978; DB03783; DB00780; DB01174; DB00946; DB00191; DB00812; DB00252; DB13878; DB01085; DB05316; DB00337; DB01100; DB06762; DB09090; DB01132; DB13941; DB12582; DB01621; DB04951; DB17472; DB11642; DB04977; DB12240; DB08910; DB08901; DB12016; DB01263; DB05478; DB15822; DB01411; DB06209; DB01588; DB01058; DB01130; DB00860; DB15566; DB14633; DB14631; DB00635; DB14646; DB13208; DB02789; DB04825; DB05154; DB01087; DB00794; DB01032; DB00396; DB00420; DB13602; DB09288; DB01182; DB12278; DB00571; DB06480; DB00545; DB01589; DB04216; DB01224; DB01103; DB13685; DB00908; DB00468; DB01369; DB12874; DB01129; DB00481; DB00980; DB00863; DB00243; DB00234; DB08896; DB11853; DB06458; DB14761; DB00409; DB00912; DB16826; DB02709; DB01256; DB13174; DB11730; DB06233; DB00615; DB04934; DB01045; DB11753; DB01201; DB01220; DB08864; DB12457; DB00896; DB06155; DB08931; DB14840; DB15305; DB00734; DB14924; DB00503; DB06228; DB09200; DB00533; DB01656; DB13409; DB09291; DB06176; DB00296; DB00412; DB05271; DB00778; DB12332; DB06201; DB11614; DB01698; DB08877; DB06654; DB12391; DB01001; DB00938; DB12543; DB01232; DB11805; DB11767; DB06335; DB00747; DB12834; DB14583; DB11459; DB01037; DB05885; DB11362; DB11942; DB15685; DB11689; DB06731; DB06739; DB06144; DB01104; DB01236; DB01105; DB00203; DB06207; DB09036; DB06290; DB00641; DB12371; DB00877; DB01261; DB06268; DB05482; DB01591; DB09308; DB09099; DB09143; DB00398; DB12713; DB15569; DB12548; DB01323; DB09118; DB00708; DB00359; DB01015; DB01138; DB01268; DB09034; DB09317; DB09318; DB00864; DB00820; DB00675; DB00706; DB06083; DB09071; DB01349; DB08833; DB12887; DB12020; DB05521; DB00976; DB12095; DB00231; DB06287; DB11761; DB00444; DB09299; DB15133; DB00857; DB00342; DB13399; DB13725; DB04905; DB00624; DB13943; DB13944; DB01420; DB13946; DB00759; DB12093; DB14066; DB11712; DB01041; DB00277; DB01154; DB00599; DB04572; DB00906; DB09289; DB08816; DB11470; DB00911; DB01007; DB01409; DB00932; DB06137; DB16732; DB11800; DB06273; DB11635; DB11251; DB08895; DB08811; DB09216; DB01036; DB06212; DB00273; DB01685; DB00539; DB05109; DB00193; DB08911; DB07615; DB00752; DB14962; DB05773; DB00656; DB00755; DB00620; DB00897; DB12245; DB12808; DB09089; DB00347; DB00440; DB06045; DB00197; DB13179; DB11652; DB15328; DB06267; DB08867; DB14989; DB13609; DB15091; DB01586; DB12255; DB11915; DB00580; DB00313; DB15114; DB05294; DB03701; DB04894; DB00862; DB11613; DB08881; DB11581; DB00285; DB00661; DB14895; DB06652; DB09082; DB06684; DB09185; DB00570; DB00541; DB00309; DB11641; DB00361; DB12131; DB08828; DB11094; DB00163; DB11693; DB11739; DB09030; DB00582; DB09068; DB14975; DB12026; DB00682; DB13950; DB01392; DB00549; DB00962; DB15035; DB15688; DB00495; DB00744; DB04832; DB00246; DB00425; DB04828; DB00909; DB01198; DB09225; DB01624; DB15490

O15287; Q6ZQX7-4

EC 1.14.14.-

3D-structure; Direct protein sequencing; Disease variant; Endoplasmic reticulum; Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Proteomics identification; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix; Ubl conjugation

A

52195.6

456

0.11

44.02

8.48

4.36

-8.85

CAMKK2

Homo sapiens (Human)

KIAA0787; Calcium/calmodulin-dependent protein kinase kinase beta; Calcium/calmodulin-dependent protein kinase kinase 2; CaMKK beta; CaMKK 2; CaM-kinase kinase beta; CaM-kinase kinase 2; CaM-KK beta;

Protein kinase superfamily, Ser/Thr protein kinase family

Kinase

Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.

Squalene synthase deficiency (SQSD) [MIM:618156]: An autosomal recessive disorder characterized by profound developmental delay, brain abnormalities, 2/3 syndactyly of the toes, facial dysmorphisms, low total and LDL-cholesterol, and abnormal urine organic acids. {ECO:0000269|PubMed:29909962}. The disease is caused by variants affecting the gene represented in this entry.

DB12010

NA

EC 2.7.11.17

3D-structure; Acetylation; Alternative splicing; ATP-binding; Calmodulin-binding; Cell projection; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; Serine/threonine-protein kinase; Transferase

A

29603.8

259

0.09

26.4

5.32

-8.63

-8.85

DAO

Homo sapiens (Human)

Daminoacid oxidase; DAMOX; DAAO

DAMOX/DASOX family

CH-NH(2) donor oxidoreductase

Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.

Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. {ECO:0000269|PubMed:12364586}. Disease susceptibility may be associated with variants affecting the gene represented in this entry.; DISEASE: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:20368421, ECO:0000269|PubMed:20538972, ECO:0000269|PubMed:22203986, ECO:0000269|PubMed:23219954, ECO:0000269|PubMed:24138986, ECO:0000269|PubMed:25701391, ECO:0000269|PubMed:37558109, ECO:0000269|PubMed:38035964, ECO:0000269|PubMed:38134563}. Disease susceptibility may be associated with variants affecting the gene represented in this entry.

DB07979; DB02838; DB04166; DB03793; DB03225; DB03147; DB03531; DB02988

Q9P2K6; O43741

EC 1.4.3.3

3D-structure; Amyotrophic lateral sclerosis; Cell projection; Cytoplasm; Disease variant; FAD; Flavoprotein; Neurodegeneration; Oxidoreductase; Peroxisome; Phosphoprotein; Proteomics identification; Reference proteome; S-nitrosylation; Schizophrenia; Secreted; Synapse

A,B

38654.6

340

0.11

29.13

6.18

-4.45

-8.84

THRA

Homo sapiens (Human)

V-erbA-related protein 7; THRA2; THRA1; Nuclear receptor subfamily 1 group A member 1; NR1A1; ERBA1; EAR7; EAR-7; C-erbA-alpha; C-erbA-1

Nuclear hormone receptor family, NR1 subfamily

Nuclear hormone receptor

High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. Isoform Alpha-1: Nuclear hormone receptor that can act as a repressor or activator of transcription.

Hypothyroidism, congenital, non-goitrous, 6 (CHNG6) [MIM:614450]: A disease characterized by growth retardation, developmental retardation, skeletal dysplasia, borderline low thyroxine levels and high triiodothyronine levels. There is differential sensitivity to thyroid hormone action, with retention of hormone responsiveness in the hypothalamic pituitary axis and liver but skeletal, gastrointestinal, and myocardial resistance. {ECO:0000269|PubMed:22168587, ECO:0000269|PubMed:24969835, ECO:0000269|PubMed:25670821, ECO:0000269|PubMed:26037512}. The disease is caused by variants affecting the gene represented in this entry.

DB01118; DB00509; DB04855; DB05035; DB03176; DB00451; DB00279; DB01583; DB05235; DB09100

Q9Y2J4; Q9Y2J4-4; O95971; Q8TAP6; Q96JM7; Q15648; Q6FHY5; P31321; Q96A49; O75410-7; Q9JLI4

NA

3D-structure; Alternative splicing; Congenital hypothyroidism; Cytoplasm; Disease variant; DNA-binding; Metal-binding; Nucleus; Proteomics identification; Receptor; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger

A

29910.1

267

0.07

52.75

5.31

-11.32

-8.84

fpr

Escherichia coli (strain K12)

NA

mvrA;b3924;JW3895

Ferredoxin--NADP reductase type 1 family

Flavoprotein

FAD binding.Ferredoxin-NADP+ reductase activity.Oxidoreductase activity.

Noonan syndrome 13 (NS13) [MIM:619087]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. NS13 inheritance is autosomal dominant. There is considerable variability in severity. {ECO:0000269|PubMed:32721402}. The disease is caused by variants affecting the gene represented in this entry.

DB03147

NA

1.18.1.2; 1.19.1.1

3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NADP; Nucleotide-binding; Oxidoreductase; Reference proteome

A

27346.2

244

0.08

30.68

7.25

0.42

-8.84

nadB

Escherichia coli (strain K12)

NA

JW2558;nicB;b2574

FAD-dependent oxidoreductase 2 family, NadB subfamily

Oxidoreductase

Flavin adenine dinucleotide binding.L-aspartate:fumarate oxidoreductase activity.L-aspartate oxidase activity.

Thyroid hormone resistance, generalized, autosomal dominant (GRTHD) [MIM:188570]: An autosomal dominant disease characterized by high levels of circulating thyroid hormones (T3-T4), goiter, abnormal mental functions, increased susceptibility to infections, abnormal growth and bone maturation, tachycardia and deafness. Affected individuals may also have attention deficit-hyperactivity disorders (ADHD) and language difficulties. Patients have normal or slightly elevated thyroid stimulating hormone (TSH). {ECO:0000269|PubMed:10660344, ECO:0000269|PubMed:12511610, ECO:0000269|PubMed:12554782, ECO:0000269|PubMed:1314846, ECO:0000269|PubMed:1324420, ECO:0000269|PubMed:1563081, ECO:0000269|PubMed:1587388, ECO:0000269|PubMed:1619012, ECO:0000269|PubMed:1661299, ECO:0000269|PubMed:16804041, ECO:0000269|PubMed:1846005, ECO:0000269|PubMed:19268523, ECO:0000269|PubMed:2153155, ECO:0000269|PubMed:2510172, ECO:0000269|PubMed:7833659, ECO:0000269|PubMed:8175986, ECO:0000269|PubMed:8514853, ECO:0000269|PubMed:8664910, ECO:0000269|PubMed:8889584}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Thyroid hormone resistance, generalized, autosomal recessive (GRTHR) [MIM:274300]: An autosomal recessive disorder characterized by goiter, clinical euthyroidism, end-organ unresponsiveness to thyroid hormone, abnormal growth and bone maturation, and deafness. Patients also have high levels of circulating thyroid hormones, with elevated thyroid stimulating hormone. {ECO:0000269|PubMed:1653889}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Selective pituitary thyroid hormone resistance (PRTH) [MIM:145650]: Variant form of thyroid hormone resistance and is characterized by clinical hyperthyroidism, with elevated free thyroid hormones, but inappropriately normal serum TSH. Unlike GRTH, where the syndrome usually segregates with a dominant allele, the mode of inheritance in PRTH has not been established. {ECO:0000269|PubMed:7528740, ECO:0000269|PubMed:8381821}. The disease is caused by variants affecting the gene represented in this entry.

DB03147

NA

1.4.3.16; 1.5.99.-

3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome

A

58993.2

529

0.07

36.96

5.76

-15.84

-8.83

treA

Escherichia coli (strain K12)

NA

JW1186;osmA;b1197

Glycosyl hydrolase 37 family

NA

Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.

SRC kinase activity has been shown to be increased in several tumor tissues and tumor cell lines such as colon carcinoma cells. {ECO:0000269|PubMed:2498394, ECO:0000269|PubMed:3093483}.; DISEASE: Thrombocytopenia 6 (THC6) [MIM:616937]: A form of thrombocytopenia, a hematologic disorder defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. THC6 is an autosomal dominant form. Affected individuals may also have bone abnormalities and an increased risk for myelofibrosis. {ECO:0000269|PubMed:26936507}. The disease is caused by variants affecting the gene represented in this entry.

NA

NA

3.2.1.28

3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Periplasm; Reference proteome; Signal

A

57508.9

507

0.11

48.32

5.48

-10.13

-8.83