NT5E

Homo sapiens (Human)

NT5; CD73 antigen; 5'-nucleotidase; 5'-NT

5'-nucleotidase family

Phosphoric monoester hydrolase

Exhibits AMP-, NAD-, and NMN-nucleosidase activities. Hydrolyzes extracellular nucleotides into membrane permeable nucleosides.

Calcification of joints and arteries (CALJA) [MIM:211800]: A condition characterized by adult-onset calcification of the lower extremity arteries, including the iliac, femoral and tibial arteries, and hand and foot capsule joints. Age of onset has been reported as early as the second decade of life, usually involving intense joint pain or calcification in the hands. {ECO:0000269|PubMed:21288095, ECO:0000269|PubMed:24887587}. The disease is caused by variants affecting the gene represented in this entry.

DB00987; DB00806

Q9Y225-2; Q8WWF5

EC 3.1.3.5

3D-structure; Alternative splicing; Cell membrane; Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding; Nucleotide-binding; Proteomics identification; Reference proteome; Signal; Zinc

A

24417.6

219

0.09

40.43

5.49

-5.75

-6.07

Malaria Adss

Plasmodium falciparum

IMP--aspartate ligase; Adenylosuccinate synthase; AdSS; AMPSase

Adenylosuccinate synthetase family

Carbon-nitrogen ligase

Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.

Hypertension and brachydactyly syndrome (HTNB) [MIM:112410]: A syndrome characterized by brachydactyly type E, severe salt-independent but age-dependent hypertension, an increased fibroblast growth rate, neurovascular contact at the rostral-ventrolateral medulla, and altered baroreflex blood pressure regulation. It results in death from stroke before age 50 years when untreated. Brachydactyly type E is characterized by shortening of the fingers mainly in the metacarpals and metatarsals. {ECO:0000269|PubMed:25961942}. The disease is caused by variants affecting the gene represented in this entry.

DB03510; DB04315; DB02109

NA

EC 6.3.4.4

3D-structure; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis

A

47877.9

424

0.09

31.72

7.63

1.58

-6.06

PPIG

Homo sapiens (Human)

NA

NA

NA

Isomerase

Cyclosporin A binding.Peptidyl-prolyl cis-trans isomerase activity.RNA binding.

Intellectual developmental disorder, autosomal dominant 6, with or without seizures (MRD6) [MIM:613970]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD6 additional features may include seizures, hypotonia, abnormal movements, such as dystonia, and autistic features. {ECO:0000269|PubMed:20890276, ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23160955, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:25356899, ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:38538865}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental and epileptic encephalopathy 27 (DEE27) [MIM:616139]: 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. {ECO:0000269|PubMed:24272827, ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:27864847, ECO:0000269|PubMed:38538865}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: A chromosomal aberrations involving GRIN2B has been found in patients with intellectual disability. Translocations t(9;12)(p23;p13.1) and t(10;12)(q21.1;p13.1) with a common breakpoint in 12p13.1.

DB00172

Q8N7W2-2; Q8NHQ1; O75553; Q9UI36-2; Q96C98; Q8NC69; P17931; Q6NVH9; Q15365; Q9UL42; Q96CD2; Q14498; Q16637; Q12800; Q9NVV9; PRO_0000037309 [P0C6X7]

5.2.1.8

3D-structure; Alternative splicing; Isomerase; Isopeptide bond; Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; Rotamase; Ubl conjugation

A

19125.4

173

0.1

26.46

7.14

0.24

-6.05

ATIC

Homo sapiens (Human)

PURH; OK/SW-cl.86; Bifunctional purine biosynthesis protein PURH

PurH family

Methyltransferase

Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.

AICA-ribosuria due to ATIC deficiency (AICAR) [MIM:608688]: A neurologically devastating inborn error of purine biosynthesis. Patients excrete massive amounts of AICA-riboside in the urine and accumulate AICA-ribotide and its derivatives in erythrocytes and fibroblasts. Clinical features include profound intellectual disability, epilepsy, dysmorphic features and congenital blindness. AICAR inheritance is autosomal recessive. {ECO:0000269|PubMed:15114530}. The disease is caused by variants affecting the gene represented in this entry.

DB02309; DB03442; DB01700; DB01972; DB00563; DB04057; DB00642; DB00116

NA

NA

3D-structure; Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing; Disease variant; Epilepsy; Hydrolase; Intellectual disability; Multifunctional enzyme; Proteomics identification; Purine biosynthesis; Reference proteome; Transferase

A,B

128556

1177

0.07

38.21

6.28

-7.98

-6.05

DAG1

Homo sapiens (Human)

Dystrophin-associated glycoprotein 1; Alpha-dystroglycan

NA

Dystroglycan protein

The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.

Muscular dystrophy-dystroglycanopathy limb-girdle C9 (MDDGC9) [MIM:613818]: An autosomal recessive muscular dystrophy showing onset in early childhood, and associated with intellectual disability without structural brain anomalies. {ECO:0000269|PubMed:21388311, ECO:0000269|PubMed:25503980}. The disease is caused by variants affecting the gene represented in this entry. MDDGC7 is caused by DAG1 mutations that interfere with normal post-translational processing, resulting in defective DAG1 glycosylation and impaired interactions with extracellular-matrix components. Other muscular dystrophy-dystroglycanopathies are caused by defects in enzymes involved in protein O-glycosylation.; DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A9 (MDDGA9) [MIM:616538]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound intellectual disability, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. {ECO:0000269|PubMed:24052401, ECO:0000269|PubMed:25934851}. The disease is caused by variants affecting the gene represented in this entry.

NA

P16333; Q3T1J5; PRO_0000021066 [Q14118]; P46939

NA

3D-structure; Autocatalytic cleavage; Cell membrane; Congenital muscular dystrophy; Cytoplasm; Cytoskeleton; Disease variant; Disulfide bond; Dystroglycanopathy; Glycoprotein; Host cell receptor for virus entry; Host-virus interaction; Limb-girdle muscular dystrophy; Lissencephaly; Membrane; Nucleus; Phosphoprotein; Postsynaptic cell membrane; Proteomics identification; Receptor; Reference proteome; Secreted; Signal; Synapse; Transmembrane; Transmembrane helix

A,C

62559.7

546

0.11

38.37

9

10.42

-6.06

Malaria Adss

Plasmodium falciparum

IMP--aspartate ligase; Adenylosuccinate synthase; AdSS; AMPSase

Adenylosuccinate synthetase family

Carbon-nitrogen ligase

Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.

Hypertension and brachydactyly syndrome (HTNB) [MIM:112410]: A syndrome characterized by brachydactyly type E, severe salt-independent but age-dependent hypertension, an increased fibroblast growth rate, neurovascular contact at the rostral-ventrolateral medulla, and altered baroreflex blood pressure regulation. It results in death from stroke before age 50 years when untreated. Brachydactyly type E is characterized by shortening of the fingers mainly in the metacarpals and metatarsals. {ECO:0000269|PubMed:25961942}. The disease is caused by variants affecting the gene represented in this entry.

DB03510; DB04315; DB02109

NA

EC 6.3.4.4

3D-structure; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis

A

47877.9

424

0.09

31.72

7.63

1.58

-6.06

USP2

Homo sapiens (Human)

Ubiquitin-specific-processing protease 2; Ubiquitin thioesterase 2; UBP41; Deubiquitinating enzyme 2; 41 kDa ubiquitin-specific protease

Peptidase C19 family, USP2 subfamily

Peptidase

Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues. Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability. Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and ARNTL/BMAL1. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells. Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1.

Defects in AKT2 are a cause of susceptibility to breast cancer (BC). AKT2 promotes metastasis of tumor cells without affecting the latency of tumor development. May play a role in glioblastoma cell survival (PubMed:20167810). {ECO:0000269|PubMed:20167810}.; DISEASE: Type 2 diabetes mellitus (T2D) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:15166380, ECO:0000269|PubMed:19164855}. Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Hypoinsulinemic hypoglycemia with hemihypertrophy (HIHGHH) [MIM:240900]: A disorder characterized by hypoglycemia, low insulin levels, low serum levels of ketone bodies and branched-chain amino acids, left-sided hemihypertrophy, neonatal macrosomia, reduced consciousness and hypoglycemic seizures. {ECO:0000269|PubMed:21979934}. The disease is caused by variants affecting the gene represented in this entry.

NA

Q9NYB9-2; P12814; P35609; Q08043; Q86U10; Q86V38; P56945; Q8TD16-2; Q96CA5; A2RRN7; Q13137; Q9H257-2; Q96JN2-2; Q2TAC2; A6NC98; Q96MT8-3; Q8NHQ1; Q9BSW2; Q8N4Y2-3; Q8WTU0; O75140-2; Q9NRI5-2; Q8N9I9; Q9H596; Q8WWB3; Q5JST6; Q9NRA8; O00471; Q96B26; P57678; Q08379; Q9NYA3; A6NEM1; Q6PI77; Q14451-3; Q4V328; Q9NSC5; Q9UJC3; Q96ED9-2; Q8IYA8; Q9UKT9; Q5TA45; Q96N16; O75564-2; Q674X7-2; Q9BVG8; Q9BVG8-5; P19012; Q7Z3Y8; Q15323; Q14525; O76011; Q92764; Q6A162; Q9UBR4-2; Q969G2; Q03252; Q9BRK4; Q00987; Q9UJV3-2; Q5VZ52; Q13084; Q5JR59; Q5JR59-3; Q15742; Q9GZM8; I6L9F6; P07196; O43482; Q96CV9; Q4G0R1; Q9NRD5; Q58EX7; Q8ND90; Q16633; Q9GZV8; Q6MZQ0; Q15276; Q8HWS3; Q59EK9-3; P60903; O14492-2; O60504; Q99932-2; A6NLX3; P51692; Q86VP1; Q8WW24; Q9UBB9; Q08117-2; Q03169; Q13077; Q12933; Q9Y4K3; P36406; P14373; Q86XT4; Q15654; Q8N6Y0; Q70EL1-9; Q9UK41-2; Q8N1B4; O96006; Q9NZV7; Q9UGI0; P05067; P54253; G5E9A7; Q01658; Q00403; Q9Y5Q9; P04792; O43464; P42858; Q8WXH2; O60333-2; A0A6Q8PF08; O60260-5; P60891; Q9Y3C5; Q7Z333; P37840; P00441; Q7Z699; Q13148; O76024

EC 3.4.19.12

3D-structure; Alternative splicing; Biological rhythms; Cell cycle; Cytoplasm; Hydrolase; Membrane; Metal-binding; Myogenesis; Nucleus; Protease; Proteomics identification; Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc

A

37785.5

327

0.11

42.45

8.23

3.56

-6.06

VDR

Homo sapiens (Human)

Vitamin D(3) receptor; Nuclear vitamin D receptor; Nuclear receptor subfamily 1 group I member 1; NR1I1; 1,25-dihydroxyvitamin D3 receptor

Nuclear hormone receptor family, NR1 subfamily

Nuclear hormone receptor

Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3-responsive target genes. Plays a central role in calcium homeostasis. Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells.

Rickets vitamin D-dependent 2A (VDDR2A) [MIM:277440]: A disorder of vitamin D metabolism resulting in severe rickets, hypocalcemia and secondary hyperparathyroidism. Most patients have total alopecia in addition to rickets. {ECO:0000269|PubMed:1652893, ECO:0000269|PubMed:17970811, ECO:0000269|PubMed:2177843, ECO:0000269|PubMed:2849209, ECO:0000269|PubMed:28698609, ECO:0000269|PubMed:7828346, ECO:0000269|PubMed:8106618, ECO:0000269|PubMed:8381803, ECO:0000269|PubMed:8392085, ECO:0000269|PubMed:8675579, ECO:0000269|PubMed:8961271, ECO:0000269|PubMed:9005998}. The disease is caused by variants affecting the gene represented in this entry.

DB07530; DB08742; DB01436; DB04891; DB00146; DB02300; DB00136; DB00169; DB04540; DB05024; DB11672; DB14635; DB01070; DB06410; DB05295; DB06194; DB00153; DB04796; DB03451; DB00910; DB04258; DB11094

P35222; Q09472; Q15648; P50222; Q15788; P26045; P19793; Q13573; Q13501; P04637; Q15645; Q9JLI4; P28700; X5D778; Q96HA8; Q01804; Q96S38; P48443

NA

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

A

28781

254

0.07

47.69

6.15

-3.44

-6.04

ACAA1

Homo sapiens (Human)

NA

PTHIO;ACAA

Thiolase-like superfamily, Thiolase family

Transferase

Acetate CoA-transferase activity.Acetyl-CoA C-acyltransferase activity.Palmitoyl-CoA oxidase activity.

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.

NA

Q9BSK4; Q12800

2.3.1.155; 2.3.1.16; 2.3.1.9

3D-structure; Acyltransferase; Alternative splicing; Fatty acid metabolism; Lipid metabolism; Peroxisome; Phosphoprotein; Proteomics identification; Reference proteome; Transferase; Transit peptide

A,B

37940.2

364

0.04

41.27

8.59

3.99

-6.05

PTPN1

Homo sapiens (Human)

Tyrosine-protein phosphatase non-receptor type 1; PTP-1B

Protein-tyrosine phosphatase family, Non-receptor class 1 subfamily

Phosphoric monoester hydrolase

Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET. Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response.

Can contribute to cancer cell survival, proliferation, migration, and invasion, and tumor angiogenesis and metastasis. May contribute to cancer pathogenesis by promoting inflammatory responses and recruitment of tumor-infiltrating macrophages.; DISEASE: Abnormally high expression of soluble isoforms (isoform 2, isoform 3 or isoform 4) may be a cause of preeclampsia.

DB08549; DB08783; DB03483; DB08593; DB04800; DB03670; DB03102; DB02072; DB02622; DB07295; DB04088; DB01820; DB02259; DB03311; DB04142; DB02620; DB07298; DB01734; DB08147; DB03557; DB07197; DB06829; DB07130; DB03714; DB07480; DB02014; DB07730; DB08001; DB07134; DB08591; DB07289; DB08397; DB04001; DB02827; DB07719; DB06887; DB04204; DB02420; DB07263; DB02615; DB03982; DB06521; DB05506; DB08003; DB03661; DB04525; DB02784; DB07651; DB02662; DB08371; DB02977; DB06333; DB02436; DB04285; DB02651; DB03154

Q13520; P56945; P11274-1; P07384; Q03135; Q14247; P00533; Q9GZR5; P19235; P10912; P62993; P08069; P06213; P06213-1; P05556; P05106; O60674; O43561; P08581; P04629; Q16288; P09619; P57054; P08922; P12931; P40763; P42229; Q9NPL8; Q96HV5; Q8N661; Q9H1D0; P10599; Q61140; Q63767; P15116; Q63768; P62994; P35570; P05622; P10686; P34152; Q8VI36; Q9WUD9; P63166

EC 3.1.3.48

3D-structure; Acetylation; Direct protein sequencing; Endoplasmic reticulum; Hydrolase; Membrane; Oxidation; Phosphoprotein; Protein phosphatase; Proteomics identification; Reference proteome; S-nitrosylation

A

34541

297

0.1

35.91

5.91

-5.37

-6.04

PPIG

Homo sapiens (Human)

NA

NA

NA

Isomerase

Cyclosporin A binding.Peptidyl-prolyl cis-trans isomerase activity.RNA binding.

Intellectual developmental disorder, autosomal dominant 6, with or without seizures (MRD6) [MIM:613970]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD6 additional features may include seizures, hypotonia, abnormal movements, such as dystonia, and autistic features. {ECO:0000269|PubMed:20890276, ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23160955, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:25356899, ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:38538865}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental and epileptic encephalopathy 27 (DEE27) [MIM:616139]: 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. {ECO:0000269|PubMed:24272827, ECO:0000269|PubMed:27839871, ECO:0000269|PubMed:27864847, ECO:0000269|PubMed:38538865}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: A chromosomal aberrations involving GRIN2B has been found in patients with intellectual disability. Translocations t(9;12)(p23;p13.1) and t(10;12)(q21.1;p13.1) with a common breakpoint in 12p13.1.

DB00172

Q8N7W2-2; Q8NHQ1; O75553; Q9UI36-2; Q96C98; Q8NC69; P17931; Q6NVH9; Q15365; Q9UL42; Q96CD2; Q14498; Q16637; Q12800; Q9NVV9; PRO_0000037309 [P0C6X7]

5.2.1.8

3D-structure; Alternative splicing; Isomerase; Isopeptide bond; Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; Rotamase; Ubl conjugation

A

19125.4

173

0.1

26.46

7.14

0.24

-6.04

CYP3A4

Homo sapiens (Human)

NA

CYP3A3

Cytochrome P450 family

Oxidoreductase

1,8-cineole 2-exo-monooxygenase activity.Albendazole monooxygenase activity.Aromatase activity.Caffeine oxidase activity.Enzyme binding.Estrogen 16-alpha-hydroxylase activity.Heme binding.Iron ion binding.Monooxygenase activity.Oxidoreductase activity.Oxygen binding.Quinine 3-monooxygenase activity.Steroid binding.Steroid hydroxylase activity.Taurochenodeoxycholate 6alpha-hydroxylase activity.Testosterone 6-beta-hydroxylase activity.Vitamin D 24-hydroxylase activity.Vitamin D3 25-hydroxylase activity.

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

1.14.14.1; 1.14.14.55; 1.14.14.56; 1.14.14.73

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

52686.1

460

0.11

43.51

8.62

4.97

-6.03

TPH1

Homo sapiens (Human)

Tryptophan 5-monooxygenase 1; TRPH; TPRH

Biopterin-dependent aromatic amino acid hydroxylase family

Paired donor oxygen oxidoreductase

Responsible for addition of the -HO group (hydroxylation) to the 5 position to form the amino acid 5-hydroxytryptophan (5-HTP), which is the initial and rate-limiting step in the synthesis of the neurotransmitter serotonin.

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.

DB05199; DB00360; DB12095; DB00150

Q14457; Q96IK1-2; Q9UKB3; Q9H8Y8; O43586; O95789-4

EC 1.14.16.4

3D-structure; Alternative splicing; Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phosphoprotein; Proteomics identification; Reference proteome; Serotonin biosynthesis; Ubl conjugation

A

31138.2

271

0.13

43.43

6.73

-0.86

-6.03

ureC

Klebsiella aerogenes (Enterobacter aerogenes)

NA

NA

Metallo-dependent hydrolases superfamily, Urease alpha subunit family

Hydrolase

Nickel cation binding.Urease activity.

Can contribute to cancer cell survival, proliferation, migration, and invasion, and tumor angiogenesis and metastasis. May contribute to cancer pathogenesis by promoting inflammatory responses and recruitment of tumor-infiltrating macrophages.; DISEASE: Abnormally high expression of soluble isoforms (isoform 2, isoform 3 or isoform 4) may be a cause of preeclampsia.

DB00551; DB05265

P18316

3.5.1.5

3D-structure; Cytoplasm; Hydrolase; Metal-binding; Nickel

C

80688.3

753

0.06

28.4

5.58

-21.17

-6.03

ponA

Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

NA

SP_0369

Glycosyltransferase 51 family; Transpeptidase family

Biosynthetic protein

Penicillin binding.Peptidoglycan glycosyltransferase activity.Serine-type D-Ala-D-Ala carboxypeptidase activity.

Aminoacylase-1 deficiency (ACY1D) [MIM:609924]: An enzymatic deficiency resulting in encephalopathy, unspecific psychomotor delay, psychomotor delay with atrophy of the vermis and syringomyelia, marked muscular hypotonia or normal clinical features. Epileptic seizures are a frequent feature. All affected individuals exhibit markedly increased urinary excretion of several N-acetylated amino acids. {ECO:0000269|PubMed:16274666, ECO:0000269|PubMed:16465618, ECO:0000269|PubMed:17562838, ECO:0000269|PubMed:21414403}. The disease is caused by variants affecting the gene represented in this entry.

DB01150; DB05659

NA

2.4.99.28; 3.4.16.4

3D-structure; Antibiotic resistance; Carboxypeptidase; Cell shape; Cell wall biogenesis/degradation; Glycosyltransferase; Hydrolase; Multifunctional enzyme; Peptidoglycan synthesis; Protease; Reference proteome; Secreted; Transferase

A,C

44805.1

400

0.12

31.82

4.88

-14.68

-6.02

NAAA

Homo sapiens (Human)

Nacylsphingosine amidohydrolaselike; Nacylethanolaminehydrolyzing acid amidase subunit beta; NAAA; Acid ceramidaselike protein; ASAHlike protein

Acid ceramidase family

Carbon-nitrogen hydrolase

Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N- palmitoylethanolamine > N-myristoylethanolamine > N- lauroylethanolamine = N-stearoylethanolamine > N- arachidonoylethanolamine > N-oleoylethanolamine. Also exhibits weak hydrolytic activity against the ceramides N- lauroylsphingosine and N-palmitoylsphingosine.

Hypertriglyceridemia, transient infantile (HTGTI) [MIM:614480]: An autosomal recessive disorder characterized by onset of moderate to severe transient hypertriglyceridemia in infancy that normalizes with age. The hypertriglyceridemia is associated with hepatomegaly, moderately elevated transaminases, persistent fatty liver, and the development of hepatic fibrosis. {ECO:0000269|PubMed:22226083, ECO:0000269|PubMed:24549054}. The disease is caused by variants affecting the gene represented in this entry.

DB09061; DB14009; DB14011

NA

EC 3.5.1.-

3D-structure; Alternative splicing; Autocatalytic cleavage; Direct protein sequencing; Disulfide bond; Fatty acid metabolism; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Lysosome; Membrane; Proteomics identification; Reference proteome; Signal; Zymogen

A,B

36877.8

328

0.11

44.37

7.72

1.08

-6.02

CCR2

Homo sapiens (Human)

Monocyte chemoattractant protein 1 receptor; MCP-1-R; Chemokine receptor CCR2B; CMKBR2; CD192; CCR-2; CC-CKR-2; C-C CKR-2

G-protein coupled receptor 1 family

GPCR rhodopsin

Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion. Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B. Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation. Faciltates the export of mature thymocytes by enhancing directional movement of thymocytes to sphingosine-1-phosphate stimulation and up-regulation of S1P1R expression; signals through the JAK-STAT pathway to regulate FOXO1 activity leading to an increased expression of S1P1R. Plays an important role in mediating peripheral nerve injury-induced neuropathic pain. Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B. Mediates the recruitment of macrophages and monocytes to the injury site following brain injury. Key functional receptor for CCL2 but can also bind CCL7 and CCL12.

Polycystic lung disease (PCLUD) [MIM:219600]: An autosomal recessive disease characterized by pulmonary alveolar proteinosis, marked peribronchovascular and parenchymal lymphocytosis, peribronchiolar pulmonary fibrosis, progressive diffuse parenchymal lung cyst formation and enlargement, progressive obstructive airflow limitation, and recurrent secondary infections. Additional features may include digital clubbing, allergies, and atopic dermatitis. {ECO:0000269|PubMed:38157855}. The disease is caused by variants affecting the gene represented in this entry.

DB05159; DB11758; DB05130; DB12520

Q6S8J3; Q9BW27

NA

3D-structure; Alternative splicing; Cell membrane; Disease variant; Disulfide bond; G-protein coupled receptor; Glycoprotein; Host-virus interaction; Inflammatory response; Membrane; Phosphoprotein; Proteomics identification; Receptor; Reference proteome; Sulfation; Transducer; Transmembrane; Transmembrane helix

A

50270.6

445

0.13

29.96

9.49

17.19

-6.02

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

-6.03

GABBR1

Homo sapiens (Human)

NA

GPRC3B;GPR51

G-protein coupled receptor 3 family, GABA-B receptor subfamily

Signaling protein / antagonist

G-protein coupled GABA receptor activity.

Neurodevelopmental disorder with poor language and loss of hand skills (NDPLHS) [MIM:617903]: An autosomal dominant disorder characterized by psychomotor developmental stagnation or regression. NDPLHS manifest in the first years of life as loss of purposeful hand movements, loss of language, and intellectual disability. {ECO:0000269|PubMed:26740508, ECO:0000269|PubMed:28856709, ECO:0000269|PubMed:29369404}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental and epileptic encephalopathy 59 (DEE59) [MIM:617904]: 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. DEE59 is an autosomal dominant condition characterized by onset of refractory seizures in early infancy. {ECO:0000269|PubMed:28856709, ECO:0000269|PubMed:29100083, ECO:0000269|PubMed:29369404}. The disease is caused by variants affecting the gene represented in this entry.

DB08891; DB08892; DB00181; DB00363; DB02530; DB05010; DB09072

Q9UBS5; Q9UBS5-2; P46459; Q86UR5

NA

3D-structure; Cell membrane; Coiled coil; Direct protein sequencing; Disease variant; Disulfide bond; Epilepsy; G-protein coupled receptor; Glycoprotein; Intellectual disability; Membrane; Phosphoprotein; Postsynaptic cell membrane; Proteomics identification; Receptor; Reference proteome; Signal; Synapse; Transducer; Transmembrane; Transmembrane helix

A

46502.1

408

0.12

50.05

5.78

-5.62

-6.01

RNGTT

Homo sapiens (Human)

NA

CAP1A

Non-receptor class of the protein-tyrosine phosphatase family; Eukaryotic GTase family

Transferase

GTP binding.MRNA guanylyltransferase activity.Polynucleotide 5'-phosphatase activity.Protein tyrosine/serine/threonine phosphatase activity.Protein tyrosine phosphatase activity.RNA guanylyltransferase activity.Triphosphatase activity.

Atrial fibrillation, familial, 14 (ATFB14) [MIM:615378]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure. {ECO:0000269|PubMed:19808477}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Genetic variations in SCN2B may be involved in Brugada syndrome (PubMed:23559163). This tachyarrhythmia is characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:23559163}.

NA

Q92624; P16333-1

2.7.7.50; 3.6.1.74

3D-structure; Alternative splicing; GTP-binding; Host-virus interaction; Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Protein phosphatase; Proteomics identification; Reference proteome; Transferase

A,B,C,D

21849.8

189

0.11

53.71

5.89

-2.91

-6.01