FDPS

Homo sapiens (Human)

KIAA1293; Geranylgeranyl pyrophosphate synthase; Geranylgeranyl diphosphate synthase; GGPS1; GGPPSase; GGPP synthase; Farnesyltranstransferase; Farnesyl pyrophosphate synthase; Farnesyl diphosphate sy

FPP/GGPP synthase family

Alkyl aryl transferase

FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones.

Porokeratosis 9, multiple types (POROK9) [MIM:616631]: A form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported. {ECO:0000269|PubMed:26202976}. The disease is caused by variants affecting the gene represented in this entry.

DB00630; DB01785; DB07780; DB02552; DB07841; DB00710; DB06255; DB04714; DB02508; DB06548; DB00282; DB00884; DB00399

O95870; P54253; Q6ZMZ0; Q9BRI3; Q8WWF3

EC 2.5.1.10

3D-structure; Acetylation; Alternative splicing; Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm; Disease variant; Host-virus interaction; Hydroxylation; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding; Proteomics identification; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase

A

38705

338

0.12

44.66

5.1

-9.92

-5.45

HIV nef

Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2) (HIV-1)

nef; Nef protein; F-protein; 3'ORF; 27 kDa protein

Lentivirus primate group Nef protein family

Lentivirus primate group Nef

Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors.

Neurodegeneration due to cerebral folate transport deficiency (NCFTD) [MIM:613068]: An autosomal recessive neurodegenerative disorder resulting from brain-specific folate deficiency early in life. Onset is apparent in late infancy with severe developmental regression, movement disturbances, epilepsy and leukodystrophy. {ECO:0000269|PubMed:19732866}. The disease is caused by variants affecting the gene represented in this entry.

NA

Q14457; P01730

NA

3D-structure; AIDS; Apoptosis; Early protein; Host cell membrane; Host Golgi apparatus; Host membrane; Host-virus interaction; Inhibition of host adaptive immune response by virus; Inhibition of host autophagy by virus; Inhibition of host MHC class I molecule presentation by virus; Inhibition of host MHC class II molecule presentation by virus; Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome; Secreted; SH3-binding; Viral immunoevasion; Virion; Virulence

A,B

29232.1

245

0.16

50.97

5.71

-7.32

-5.46

AOX1

Homo sapiens (Human)

AOX1

Xanthine dehydrogenase family

Aldehyde/oxo donor oxidoreductase

Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and N- methylphthalazinium, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir topenciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis.

Progressive familial heart block 1B (PFHB1B) [MIM:604559]: A cardiac bundle branch disorder characterized by progressive alteration of cardiac conduction through the His-Purkinje system, with a pattern of a right bundle-branch block and/or left anterior hemiblock occurring individually or together. It leads to complete atrio-ventricular block causing syncope and sudden death. {ECO:0000269|PubMed:19726882, ECO:0000269|PubMed:20562447, ECO:0000269|PubMed:21887725}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Erythrokeratodermia variabilis et progressiva 6 (EKVP6) [MIM:618531]: A form of erythrokeratodermia variabilis et progressiva, a genodermatosis characterized by the coexistence of two independent skin lesions: transient erythema and hyperkeratosis that is usually localized but occasionally occurs in its generalized form. Clinical presentation varies significantly within a family and from one family to another. Palmoplantar keratoderma is present in around 50% of cases. EKVP6 inheritance is autosomal dominant. {ECO:0000269|PubMed:30528822}. The disease is caused by variants affecting the gene represented in this entry.

DB00437; DB00513; DB00484; DB11791; DB00215; DB00924; DB03516; DB01175; DB00426; DB12466; DB09054; DB09078; DB00170; DB01033; DB00563; DB08840; DB00157; DB00339; DB00481; DB04827; DB00962; DB00246; DB00909

Q06278

EC 1.2.3.1

2Fe-2S; 3D-structure; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Lipid metabolism; Metal-binding; Molybdenum; Oxidoreductase; Phosphoprotein; Proteomics identification; Reference proteome

A,B

286845

2590

0.08

42.7

6.92

-1.62

-5.45

LANCL1

Homo sapiens (Human)

p40; LanC-like protein 1; GPR69A; 40 kDa erythrocyte membrane protein

LanC-like protein family

NA

Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (By similarity). May play a role in EPS8 signaling. Binds glutathione.

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.

NA

Q9UHR4; P42858; Q08509

EC 2.5.1.18

3D-structure; Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing; Membrane; Metal-binding; Proteomics identification; Reference proteome; Transferase; Zinc

A

46005.4

405

0.14

33.7

7.13

0.4

-5.46

HDAC7

Homo sapiens (Human)

Histone deacetylase 7A; HDAC7A; HD7a; HD7

Histone deacetylase family, HD type 2 subfamily

Carbon-nitrogen hydrolase

Gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Positively regulates the transcriptional repressor activity of FOXP3. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4).

Mucopolysaccharidosis 1H (MPS1H) [MIM:607014]: A severe form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. Patients with MPS1H usually present, within the first year of life, a combination of hepatosplenomegaly, skeletal deformities, corneal clouding and severe intellectual disability. Obstructive airways disease, respiratory infection and cardiac complications usually result in death before 10 years of age. {ECO:0000269|PubMed:10466419, ECO:0000269|PubMed:10735634, ECO:0000269|PubMed:12559846, ECO:0000269|PubMed:1301941, ECO:0000269|PubMed:15300847, ECO:0000269|PubMed:19396826, ECO:0000269|PubMed:21394825, ECO:0000269|PubMed:24036510, ECO:0000269|PubMed:31194252, ECO:0000269|PubMed:7550232, ECO:0000269|PubMed:7550242, ECO:0000269|PubMed:7951228, ECO:0000269|PubMed:8019563, ECO:0000269|PubMed:8328452, ECO:0000269|PubMed:8401515, ECO:0000269|Ref.20}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Mucopolysaccharidosis 1H/S (MPS1H/S) [MIM:607015]: A form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. MPS1H/S represents an intermediate phenotype of the MPS1 clinical spectrum. It is characterized by relatively little neurological involvement, but most of the somatic symptoms described for severe MPS1 develop in the early to mid-teens, causing considerable loss of mobility. {ECO:0000269|PubMed:10466419, ECO:0000269|PubMed:10735634, ECO:0000269|PubMed:12559846, ECO:0000269|PubMed:15300847, ECO:0000269|PubMed:21394825, ECO:0000269|PubMed:7550232, ECO:0000269|PubMed:7550242, ECO:0000269|PubMed:8401515}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Mucopolysaccharidosis 1S (MPS1S) [MIM:607016]: A mild form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. Patients with MPS1S may have little or no neurological involvement, normal stature and life span, but present development of joints stiffness, mild hepatosplenomegaly, aortic valve disease and corneal clouding. {ECO:0000269|PubMed:12559846, ECO:0000269|PubMed:15300847, ECO:0000269|PubMed:19396826, ECO:0000269|PubMed:21394825, ECO:0000269|PubMed:25256405, ECO:0000269|PubMed:7550232, ECO:0000269|PubMed:7550242, ECO:0000269|PubMed:8213840}. The disease is caused by variants affecting the gene represented in this entry.

DB12565; DB05015; DB01262; DB11841; DB12645; DB06603; DB06819; DB03766; DB12847; DB06176; DB04297; DB00313; DB02546

P00533; Q9BZS1-1; Q9BZS1-2; Q9BZL6; P31947; P63104; P08393; Q8CFN5; Q13137; Q04864; Q0D2K3; Q8WXI4-2; Q9BQD7; Q03989; Q9NSI6-4; Q3SXR2; Q13137; P60953; Q7L2Z9; Q96D03; Q9NQ30; Q9UBI6; A6NEM1; A5PKX9; Q9BXK1; Q6ZNG9; O43679; Q6FHY5; Q9BRT3; O94964-4; O95411; O00746; Q9BQI9; B7ZLY0; Q96I34; P63000; P15153; P60763; Q04864-2; Q0D2K3; P62070; O15427; O95164

EC 3.5.1.98

3D-structure; Alternative splicing; Chromatin regulator; Cytoplasm; Hydrolase; Metal-binding; Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Zinc

A

41454.5

383

0.08

38.49

6.26

-5.18

-5.45

RPS6KA6

Homo sapiens (Human)

pp90RSK4; p90RSK6; p90-RSK 6; S6K-alpha-6; Ribosomal S6 kinase 4; RSK4; RSK-4; 90 kDa ribosomal protein S6 kinase 6

Protein kinase superfamily, AGC Ser/Thr protein kinase family, S6 kinase subfamily

NA

Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis.

Symptomatic deficiency in lactate transport (SDLT) [MIM:245340]: Deficiency of lactate transporter may result in an acidic intracellular environment created by muscle activity with consequent degeneration of muscle and release of myoglobin and creatine kinase. This defect might compromise extreme performance in otherwise healthy individuals. {ECO:0000269|PubMed:10590411}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hyperinsulinemic hypoglycemia, familial, 7 (HHF7) [MIM:610021]: A form of hyperinsulinemic hypoglycemia, a clinically and genetically heterogeneous disorder characterized by inappropriate insulin secretion from the pancreatic beta-cells in the presence of low blood glucose levels. HHF7 features include exercise-induced hyperinsulinism, loss of consciousness due to hypoglycemia, and hypoglycemic seizures. HHF7 inheritance is autosomal dominant. {ECO:0000269|PubMed:17701893}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Monocarboxylate transporter 1 deficiency (MCT1D) [MIM:616095]: A metabolic disorder characterized by recurrent ketoacidosis, a pathologic state due to ketone formation exceeding ketone utilization. The clinical consequences of ketoacidosis are vomiting, osmotic diuresis, dehydration, and Kussmaul breathing. The condition may progress to decreased consciousness and, ultimately, death. {ECO:0000269|PubMed:25390740}. The disease is caused by variants affecting the gene represented in this entry.

DB12010

Q7Z698

EC 2.7.11.1

3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase

A

33406.4

291

0.11

38.08

8.4

2.55

-5.45

R

Escherichia phage lambda (Bacteriophage lambda)

NA

NA

Glycosyl hydrolase 24 family

Glycosidase

Lyase activity.Lysozyme activity.Lytic transglycosylase activity.

Estrogen resistance (ESTRR) [MIM:615363]: A disorder characterized by partial or complete resistance to estrogens, in the presence of elevated estrogen serum levels. Clinical features include absence of the pubertal growth spurt, delayed bone maturation, unfused epiphyses, reduced bone mineral density, osteoporosis, continued growth into adulthood and very tall adult stature. Glucose intolerance, hyperinsulinemia and lipid abnormalities may also be present. {ECO:0000269|PubMed:23841731, ECO:0000269|PubMed:27754803}. The disease is caused by variants affecting the gene represented in this entry.

DB04206

NA

4.2.2.n2

3D-structure; Antimicrobial; Bacteriolytic enzyme; Cytolysis; Direct protein sequencing; Host cell lysis by virus; Host cytoplasm; Lyase; Reference proteome; Viral release from host cell

A,B,C

49834.9

462

0.07

18.78

9.6

18.29

-5.44

ADH1C

Homo sapiens (Human)

NA

ADH3

Zinc-containing alcohol dehydrogenase family

Oxidoreductase

Alcohol dehydrogenase (NAD) activity.Alcohol dehydrogenase activity, zinc-dependent.Ethanol binding.Retinol dehydrogenase activity.Zinc ion binding.

Combined oxidative phosphorylation deficiency 6 (COXPD6) [MIM:300816]: A mitochondrial disease resulting in a neurodegenerative disorder characterized by psychomotor delay, hypotonia, areflexia, muscle weakness and wasting. Some patients manifest prenatal ventriculomegaly and severe postnatal encephalomyopathy. {ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:22019070, ECO:0000269|PubMed:25583628, ECO:0000269|PubMed:26004228, ECO:0000269|PubMed:26173962, ECO:0000269|PubMed:27178839}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, X-linked recessive, 4, with or without cerebellar ataxia (CMTX4) [MIM:310490]: A neuromuscular disorder characterized by progressive sensorimotor axonal neuropathy, distal sensory impairment, difficulty walking due to peripheral neuropathy and/or cerebellar ataxia, and deafness due to auditory neuropathy. Additional features include cognitive impairment, cerebellar atrophy, dysarthria, abnormal extraocular movements, tremor, dysmetria and spasticity. The age at onset ranges from infancy to young adulthood. {ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:26004228}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Deafness, X-linked, 5, with peripheral neuropathy (DFNX5) [MIM:300614]: A form of hearing loss characterized by absent or severely abnormal auditory brainstem response, abnormal middle ear reflexes, abnormal speech discrimination, loss of outer hair cell function, and cochlear nerve hypoplasia. DFNX5 patients manifest auditory neuropathy with childhood onset, associated with distal sensory impairment affecting the peripheral nervous system. {ECO:0000269|PubMed:25986071}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spondyloepimetaphyseal dysplasia, X-linked, with hypomyelinating leukodystrophy (SEMDHL) [MIM:300232]: An X-linked recessive developmental disorder characterized by slowly progressive skeletal and neurologic abnormalities, including short stature, large and deformed joints, significant motor impairment, visual defects, and sometimes cognitive deficits. Affected individuals typically have normal early development in the first year or so of life, followed by development regression and the development of symptoms. Brain imaging shows white matter abnormalities consistent with hypomyelinating leukodystrophy. {ECO:0000269|PubMed:28842795}. The disease is caused by variants affecting the gene represented in this entry.

DB03061; DB01711; DB04312; DB04448; DB02249; DB02871; DB02721; DB03020; DB02659; DB04071; DB03559; DB00898; DB01213; DB02131; DB04113; DB00157; DB02822; DB02757; DB03226; DB14487; DB14533; DB14548

P00325

1.1.1.1

3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Proteomics identification; Reference proteome; Zinc

A,B

39693.9

374

0.06

23.06

8.53

5.87

-5.44

PLAU

Homo sapiens (Human)

UPA; U-plasminogen activator

Peptidase S1 family

Peptidase

Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.

Quebec platelet disorder (QPD) [MIM:601709]: An autosomal dominant bleeding disorder due to a gain-of-function defect in fibrinolysis. Although affected individuals do not exhibit systemic fibrinolysis, they show delayed onset bleeding after challenge, such as surgery. The hallmark of the disorder is markedly increased PLAU levels within platelets, which causes intraplatelet plasmin generation and secondary degradation of alpha-granule proteins. {ECO:0000269|PubMed:20007542}. The disease is caused by variants affecting the gene represented in this entry.

DB07129; DB07122; DB01905; DB02287; DB03729; DB01725; DB08072; DB07625; DB07626; DB08697; DB03136; DB01977; DB07076; DB03082; DB02705; DB02473; DB02398; DB02551; DB03865; DB06855; DB06856; DB03046; DB04059; DB04172; DB00594; DB03127; DB02526; DB03159; DB05254; DB03782; DB06857; DB16701; DB03876; DB03476

Q9UKQ2; P05067; Q03405-1; P05121; P55000

EC 3.4.21.73

3D-structure; Alternative splicing; Blood coagulation; Direct protein sequencing; Disulfide bond; EGF-like domain; Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase; Kringle; Pharmaceutical; Phosphoprotein; Plasminogen activation; Protease; Proteomics identification; Reference proteome; Secreted; Serine protease; Signal; Zymogen

U

25825.3

229

0.1

47.36

8.65

5.38

-5.45

pobA

Pseudomonas fluorescens

NA

NA

Aromatic-ring hydroxylase family

Oxidoreductase

4-hydroxybenzoate 3-monooxygenase activity.FAD binding.Flavin adenine dinucleotide binding.

Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and intellectual disability. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome. {ECO:0000269|PubMed:10486321}. The disease is caused by variants affecting the gene represented in this entry.

DB02839; DB04242; DB02059; DB02362; DB03147

NA

1.14.13.2

3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase

A

43949.7

391

0.09

34.92

6.78

-0.68

-5.44

putA

Escherichia coli (strain K12)

NA

b1014;poaA;JW0999

Proline dehydrogenase family; Aldehyde dehydrogenase family

Oxidoreductase

1-pyrroline-5-carboxylate dehydrogenase activity.Bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding.DNA binding.Flavin adenine dinucleotide binding.Identical protein binding.Proline dehydrogenase activity.Sequence-specific DNA binding.Transcriptional repressor activity, bacterial-type RNA polymerase core promoter proximal region sequence-specific binding.

Fructose-1,6-bisphosphatase deficiency (FBP1D) [MIM:229700]: An autosomal recessive metabolic disorder characterized by impaired gluconeogenesis, and episodes of hypoglycemia and metabolic acidosis that can be lethal in newborn infants or young children. {ECO:0000269|PubMed:12126934, ECO:0000269|PubMed:25601412, ECO:0000269|PubMed:9382095}. The disease is caused by variants affecting the gene represented in this entry.

DB03051; DB03147; DB04398

P09546

1.2.1.88; 1.5.5.2

3D-structure; DNA-binding; FAD; Flavoprotein; Multifunctional enzyme; NAD; Oxidoreductase; Proline metabolism; Reference proteome; Repressor; Transcription; Transcription regulation

A

45567.7

407

0.08

33.2

7.22

0.47

-5.44

F7

Homo sapiens (Human)

Serum prothrombin conversion accelerator; SPCA; Proconvertin; Eptacog alfa

Peptidase S1 family

Peptidase

Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.

Factor VII deficiency (FA7D) [MIM:227500]: A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels. {ECO:0000269|PubMed:10862079, ECO:0000269|PubMed:11091194, ECO:0000269|PubMed:11129332, ECO:0000269|PubMed:12472587, ECO:0000269|PubMed:14717781, ECO:0000269|PubMed:1634227, ECO:0000269|PubMed:18976247, ECO:0000269|PubMed:19432927, ECO:0000269|PubMed:19751712, ECO:0000269|PubMed:2070047, ECO:0000269|PubMed:21206266, ECO:0000269|PubMed:21372693, ECO:0000269|PubMed:26761581, ECO:0000269|PubMed:7974346, ECO:0000269|PubMed:7981691, ECO:0000269|PubMed:8043443, ECO:0000269|PubMed:8204879, ECO:0000269|PubMed:8242057, ECO:0000269|PubMed:8364544, ECO:0000269|PubMed:8652821, ECO:0000269|PubMed:8844208, ECO:0000269|PubMed:8883260, ECO:0000269|PubMed:8940045, ECO:0000269|PubMed:9414278, ECO:0000269|PubMed:9452082, ECO:0000269|PubMed:9576180}. The disease is caused by variants affecting the gene represented in this entry.

DB04590; DB07207; DB04758; DB04606; DB04593; DB07376; DB07247; DB08232; DB06552; DB13151; DB00100; DB13152; DB00036; DB09332; DB04767; DB13933

P13726

EC 3.4.21.21

3D-structure; Alternative splicing; Blood coagulation; Calcium; Cleavage on pair of basic residues; Direct protein sequencing; Disease variant; Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase; Hydroxylation; Pharmaceutical; Protease; Proteomics identification; Reference proteome; Repeat; Secreted; Serine protease; Signal; Zymogen

H

26492.2

240

0.09

34.61

6.81

-0.52

-5.44

TK

Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)

NA

UL23

Herpesviridae thymidine kinase family

Transferase

ATP binding.Thymidine kinase activity.

Atransferrinemia (ATRAF) [MIM:209300]: A rare autosomal recessive disorder characterized by abnormal synthesis of transferrin leading to iron overload and microcytic hypochromic anemia. {ECO:0000269|PubMed:11110675, ECO:0000269|PubMed:15466165}. The disease is caused by variants affecting the gene represented in this entry.

NA

NA

2.7.1.21

3D-structure; ATP-binding; DNA synthesis; Early protein; Kinase; Nucleotide-binding; Reference proteome; Transferase

A,B

67808.8

624

0.07

43.94

6.1

-7.02

-5.44

pchF

Pseudomonas putida (Arthrobacter siderocapsulatus)

NA

NA

NA

Oxidoreductase

4-cresol dehydrogenase (hydroxylating) activity.Flavin adenine dinucleotide binding.Oxidoreductase activity, acting on CH-OH group of donors.

Dihydrolipoamide dehydrogenase deficiency (DLDD) [MIM:246900]: An autosomal recessive metabolic disorder characterized biochemically by a combined deficiency of the branched-chain alpha-keto acid dehydrogenase complex (BCKDC), pyruvate dehydrogenase complex (PDC), and alpha-ketoglutarate dehydrogenase complex (KGDC). Clinically, affected individuals have lactic acidosis and neurologic deterioration due to sensitivity of the central nervous system to defects in oxidative metabolism. {ECO:0000269|PubMed:10448086, ECO:0000269|PubMed:11687750, ECO:0000269|PubMed:12925875, ECO:0000269|PubMed:15712224, ECO:0000269|PubMed:16442803, ECO:0000269|PubMed:16770810, ECO:0000269|PubMed:17404228, ECO:0000269|PubMed:20160912, ECO:0000269|PubMed:8506365, ECO:0000269|PubMed:8968745, ECO:0000269|PubMed:9540846, ECO:0000269|PubMed:9934985}. The disease is caused by variants affecting the gene represented in this entry.

DB03147

NA

1.17.9.1

3D-structure; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Plasmid

A

57240.8

515

0.1

30.94

6.06

-4.42

-5.44

TAT

Homo sapiens (Human)

NA

NA

Class-I pyridoxal-phosphate-dependent aminotransferase family

Transferase

Amino acid binding.L-phenylalanine:2-oxoglutarate aminotransferase activity.L-tyrosine:2-oxoglutarate aminotransferase activity.Pyridoxal phosphate binding.

Tyrosinemia 2 (TYRSN2) [MIM:276600]: An inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and intellectual disability. {ECO:0000269|PubMed:1357662}. The disease is caused by variants affecting the gene represented in this entry.

DB00142; DB00120; DB00114; DB00135

P15104; P28799; P28799-2; P17735; Q05086; Q05086-3

2.6.1.5

3D-structure; Acetylation; Aminotransferase; Disease variant; Intellectual disability; Palmoplantar keratoderma; Phenylalanine catabolism; Phosphoprotein; Proteomics identification; Pyridoxal phosphate; Reference proteome; Transferase; Tyrosine catabolism

A,B

42209.5

380

0.08

51.79

5.29

-10.66

-5.45

bglA

Paenibacillus polymyxa (Bacillus polymyxa)

NA

NA

Glycosyl hydrolase 1 family

Hydrolase

Beta-glucosidase activity.Scopolin beta-glucosidase activity.

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:15645182}. Disease susceptibility may be associated with variants affecting the gene represented in this entry.

DB02658; DB04282; DB04304

NA

3.2.1.21

3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase; Polysaccharide degradation

A

51515.2

447

0.14

38.44

5.28

-18.1

-5.44

CAD

Homo sapiens (Human)

CAD

CarA family; CarB family; Metallo-dependent hydrolases superfamily, DHOase family, CAD subfamily; Aspartate/ornithine carbamoyltransferase superfamily, ATCase family

Carbon-nitrogen ligase

This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).

Developmental and epileptic encephalopathy 50 (DEE50) [MIM:616457]: A form of epileptic encephalopathy, a heterogeneous group of severe 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. DEE50 is an autosomal recessive, progressive disease with onset in infancy and favorable response to treatment with oral uridine. {ECO:0000269|PubMed:25678555, ECO:0000269|PubMed:28087732}. The disease is caused by variants affecting the gene represented in this entry.

DB00128; DB00130; DB03459

P27708; Q8N137; P63104

NA

3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Congenital disorder of glycosylation; Cytoplasm; Direct protein sequencing; Disease variant; Epilepsy; Hydrolase; Ligase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein; Proteomics identification; Pyrimidine biosynthesis; Reference proteome; Repeat; Transferase; Zinc

A

38268.4

351

0.06

41.29

5.86

-10.56

-5.45

RRM2

Homo sapiens (Human)

NA

RR2

Ribonucleoside diphosphate reductase small chain family

Oxidoreductase

Metal ion binding.Ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor.

Pyruvate kinase hyperactivity (PKHYP) [MIM:102900]: Autosomal dominant phenotype characterized by increase of red blood cell ATP. {ECO:0000269|PubMed:9090535}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pyruvate kinase deficiency of red cells (PKRD) [MIM:266200]: A frequent cause of hereditary non-spherocytic hemolytic anemia. Clinically, pyruvate kinase-deficient patients suffer from a highly variable degree of chronic hemolysis, ranging from severe neonatal jaundice and fatal anemia at birth, severe transfusion-dependent chronic hemolysis, moderate hemolysis with exacerbation during infection, to a fully compensated hemolysis without apparent anemia. {ECO:0000269|PubMed:10087985, ECO:0000269|PubMed:10772876, ECO:0000269|PubMed:11328279, ECO:0000269|PubMed:11960989, ECO:0000269|PubMed:1536957, ECO:0000269|PubMed:1896471, ECO:0000269|PubMed:19085939, ECO:0000269|PubMed:2018831, ECO:0000269|PubMed:21794208, ECO:0000269|PubMed:7706479, ECO:0000269|PubMed:8161798, ECO:0000269|PubMed:8180378, ECO:0000269|PubMed:8476433, ECO:0000269|PubMed:8481523, ECO:0000269|PubMed:8483951, ECO:0000269|PubMed:8664896, ECO:0000269|PubMed:8807089, ECO:0000269|PubMed:9075576, ECO:0000269|PubMed:9482576, ECO:0000269|PubMed:9827908, ECO:0000269|PubMed:9886305, ECO:0000269|Ref.24}. The disease is caused by variants affecting the gene represented in this entry.

DB00242; DB05260; DB05801; DB05003; DB05428

P41002; Q9UM11; P23921; O00560

1.17.4.1

3D-structure; Alternative splicing; Cytoplasm; Deoxyribonucleotide synthesis; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Proteomics identification; Reference proteome; Ubl conjugation

A,B,C,D

33579.4

286

0.14

43.7

5.12

-12.86

-5.45

LTA4H

Homo sapiens (Human)

Leukotriene A4 hydrolase; Leukotriene A(4)Leukotriene A-4 hydrolase hydrolase; Leukotriene A(4) hydrolase; LTA4; LTA-H; LTA-4hydrolase; LTA-4 hydrolase

Peptidase M1 family

Ether bond hydrolase

Has also aminopeptidase activity. Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4.

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.

DB07102; DB06917; DB07258; DB07094; DB07259; DB02352; DB07292; DB07104; DB06828; DB08466; DB01197; DB05177; DB03366; DB08040; DB06851; DB02062; DB07099; DB07260; DB07196; DB11781; DB03424; DB07237

Q9BSI4

EC 3.3.2.6

3D-structure; Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing; Hydrolase; Leukotriene biosynthesis; Lipid metabolism; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Proteomics identification; Reference proteome; Zinc

A

68927

608

0.1

38.84

5.87

-9.86

-5.45

TF

Homo sapiens (Human)

Siderophilin; Serotransferrin; PRO1400; Beta-1 metal-binding globulin

Transferrin family

Transferrin

It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.

Atransferrinemia (ATRAF) [MIM:209300]: A rare autosomal recessive disorder characterized by abnormal synthesis of transferrin leading to iron overload and microcytic hypochromic anemia. {ECO:0000269|PubMed:11110675, ECO:0000269|PubMed:15466165}. The disease is caused by variants affecting the gene represented in this entry.

DB01370; DB14517; DB14518; DB01294; DB14526; DB14527; DB11136; DB14528; DB14529; DB14530; DB00515; DB09130; DB11397; DB13949; DB14490; DB14491; DB14488; DB14501; DB14489; DB13257; DB06215; DB06784; DB05260; DB01592; DB00893; DB00677; DB06757; DB11182; DB14520; DB01593; DB14487; DB14533; DB14548

O43315; O00501; Q7Z7G2; Q9GZR5; Q9Y282; Q96KR6; P01350; P08034; Q8NBJ4; O15529; Q8TED1; Q7Z5P4; A8MZ59; O15173; Q96TC7; Q3KNW5; Q9BXS9-3; Q99523; O43278-2; Q8N9I0; P02786; Q4KMG9; Q9K0U9; Q09057; Q9K0V0; P02786

NA

3D-structure; Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport; Metal-binding; Methylation; Phosphoprotein; Proteomics identification; Reference proteome; Repeat; Secreted; Signal; Transport

A

35854.5

324

0.1

34.17

7.58

1.42

-5.44