FCGRT

Homo sapiens (Human)

Neonatal FcR; MHC class I family-like Fc receptor; IgG Fc fragment receptor transporter, alpha chain; FcRn; FCGRT

Immunoglobulin superfamily

Immunoglobulin

Binds to the Fc region of monomericimmunoglobulins gamma. Mediates the uptake of IgG from milk. Possible role in transfer of immunoglobulin G from mother to fetus.

Lecithin-cholesterol acyltransferase deficiency (LCATD) [MIM:245900]: A disorder of lipoprotein metabolism characterized by inadequate esterification of plasmatic cholesterol. Two clinical forms are recognized: complete LCAT deficiency and fish-eye disease. LCATD is generally referred to the complete form which is associated with absence of both alpha and beta LCAT activities resulting in esterification anomalies involving both HDL (alpha-LCAT activity) and LDL (beta-LCAT activity). It causes a typical triad of diffuse corneal opacities, target cell hemolytic anemia, and proteinuria with renal failure. {ECO:0000269|PubMed:11423760, ECO:0000269|PubMed:12957688, ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:16051254, ECO:0000269|PubMed:16216249, ECO:0000269|PubMed:1681161, ECO:0000269|PubMed:1859405, ECO:0000269|PubMed:2370048, ECO:0000269|PubMed:7607641, ECO:0000269|PubMed:7711728, ECO:0000269|PubMed:8318557, ECO:0000269|PubMed:8432868, ECO:0000269|PubMed:8807342, ECO:0000269|PubMed:9007616, ECO:0000269|PubMed:9741700}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Fish-eye disease (FED) [MIM:136120]: A disorder of lipoprotein metabolism due to partial lecithin-cholesterol acyltransferase deficiency that affects only alpha-LCAT activity. FED is characterized by low plasma HDL and corneal opacities due to accumulation of cholesterol deposits in the cornea ('fish-eye'). {ECO:0000269|PubMed:1516702, ECO:0000269|PubMed:1571050, ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:1737840, ECO:0000269|PubMed:21901787, ECO:0000269|PubMed:8620346, ECO:0000269|PubMed:9261271}. The disease is caused by variants affecting the gene represented in this entry.

DB15270; DB14919

Q8N6F1-2; Q92520; Q9NZG7; Q01453; O00526

NA

3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond; Endosome; Glycoprotein; IgG-binding protein; Immunoglobulin domain; Membrane; Phosphoprotein; Proteomics identification; Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix

A,B

41031.7

362

0.12

35.47

6.08

-5.22

-5.96

Malaria DHOdehase

Plasmodium falciparum (isolate 3D7)

PFF0160c; Mitochondrially bound dihydroorotate-ubiqui oxidoreductase; Dihydroorotate oxidase of Plasmodium falciparum; Dihydroorotate dehydrogenase of Plasmodium falciparum; DHOdehase of Plasmodium fa

Dihydroorotate dehydrogenase family, Type 2 subfamily

CH-CH donor oxidoreductase

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

Combined oxidative phosphorylation deficiency 33 (COXPD33) [MIM:617713]: An autosomal recessive disorder caused by multiple mitochondrial respiratory chain defects and impaired mitochondrial energy metabolism. Clinical manifestations are highly variable. Affected infants present with cardiomyopathy accompanied by multisystemic features involving liver, kidney, and brain. Death in infancy is observed in some patients. Children and adults present with myopathy and progressive external ophthalmoplegia. {ECO:0000269|PubMed:28942965}. The disease is caused by variants affecting the gene represented in this entry.

DB01117

NA

EC 1.3.5.2

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

A

41846.8

371

0.1

37.25

8.21

3.13

-5.96

MycB mmpL3

Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Trehalose monomycolate exporter MmpL3; TMM exporter MmpL3

Resistance-nodulation-cell division (RND) (TC 2.A.6) family, MmpL subfamily

NA

Transports trehalose monomycolate (TMM) across the inner membrane. Could also be part of a heme-iron acquisition system.

Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:8955068}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:17332249}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Noonan syndrome 3 (NS3) [MIM:609942]: 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:16474405, ECO:0000269|PubMed:16773572, ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:17468812, ECO:0000269|PubMed:19396835, ECO:0000269|PubMed:20949621}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. {ECO:0000269|PubMed:14534542, ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:7773929}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Defects in KRAS are a cause of pylocytic astrocytoma (PA). Pylocytic astrocytomas are neoplasms of the brain and spinal cord derived from glial cells which vary from histologically benign forms to highly anaplastic and malignant tumors. {ECO:0000269|PubMed:16247081}.; DISEASE: Cardiofaciocutaneous syndrome 2 (CFC2) [MIM:615278]: A form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and intellectual disability. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices. CFC2 patients often do not have the skin abnormalities, such as ichthyosis, hyperkeratosis, and hemangioma observed in CFC1. {ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:16474405, ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:20949621, ECO:0000269|PubMed:21797849}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: KRAS mutations are involved in cancer development. {ECO:0000269|PubMed:14534542, ECO:0000269|PubMed:1553789, ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:24623306, ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:3627975, ECO:0000269|PubMed:6092920, ECO:0000269|PubMed:6695174, ECO:0000269|PubMed:7773929}.; DISEASE: Oculoectodermal syndrome (OES) [MIM:600268]: A syndrome characterized by the association of epibulbar dermoids and aplasia cutis congenita. Affected individuals show multiple, asymmetric, atrophic, non-scarring and hairless regions that may be associated with hamartomas. Ectodermal changes include linear hyperpigmentation that may follow the lines of Blaschko and rarely epidermal nevus-like lesions. Epibulbar dermoids may be uni-or bilateral. Additional ocular anomalies such as skin tags of the upper eyelid, rarely optic nerve or retinal changes, and microphthalmia can be present. The phenotypic expression is highly variable, and various other abnormalities have occasionally been reported including growth failure, lymphedema, cardiovascular defects, as well as neurodevelopmental symptoms like developmental delay, epilepsy, learning difficulties, and behavioral abnormalities. Benign tumor-like lesions such as nonossifying fibromas of the long bones and giant cell granulomas of the jaws have repeatedly been observed and appear to be age-dependent, becoming a common manifestation in individuals aged 5 years or older. {ECO:0000269|PubMed:25808193, ECO:0000269|PubMed:26970110, ECO:0000269|PubMed:30891959}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Schimmelpenning-Feuerstein-Mims syndrome (SFM) [MIM:163200]: A disease characterized by sebaceous nevi, often on the face, associated with variable ipsilateral abnormalities of the central nervous system, ocular anomalies, and skeletal defects. Many oral manifestations have been reported, not only including hypoplastic and malformed teeth, and mucosal papillomatosis, but also ankyloglossia, hemihyperplastic tongue, intraoral nevus, giant cell granuloma, ameloblastoma, bone cysts, follicular cysts, oligodontia, and odontodysplasia. Sebaceous nevi follow the lines of Blaschko and these can continue as linear intraoral lesions, as in mucosal papillomatosis. {ECO:0000269|PubMed:30891959}. The disease is caused by variants affecting the gene represented in this entry.

NA

NA

NA

3D-structure; Cell inner membrane; Cell membrane; Cell wall biogenesis/degradation; Lipid transport; Membrane; Reference proteome; Transmembrane; Transmembrane helix; Transport

A

77237

717

0.09

33.34

8.65

4.3

-5.96

Pseudo mdeA

Pseudomonas putida (Arthrobacter siderocapsulatus)

Pseudo MGL; L-methionine gamma-lyase; L-methioninase; Homocysteine desulfhydrase

Trans-sulfuration enzymes family, L-methionine gamma-lyase subfamily

Carbon-sulfur lyases

Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia. Is involved in L-methionine catabolism. In fact, shows a multicatalytic function since it also catalyzes gamma-replacement of L-methionine with thiol compounds, alpha,gamma-elimination and gamma-replacement reactions of L-homocysteine and its S-substituted derivatives, O-substituted-L-homoserines and DL-selenomethionine, and, to a lesser extent, alpha,beta-elimination and beta-replacement reactions of L-cysteine, S-methyl-L-cysteine, and O-acetyl-L-serine. Also catalyzes deamination and gamma-addition reactions of L-vinylglycine. Thus, the enzyme is able to cleave C-S, C-Se, and C-O bonds of sulfur, selenium, and oxygen amino acids, respectively.

Lecithin-cholesterol acyltransferase deficiency (LCATD) [MIM:245900]: A disorder of lipoprotein metabolism characterized by inadequate esterification of plasmatic cholesterol. Two clinical forms are recognized: complete LCAT deficiency and fish-eye disease. LCATD is generally referred to the complete form which is associated with absence of both alpha and beta LCAT activities resulting in esterification anomalies involving both HDL (alpha-LCAT activity) and LDL (beta-LCAT activity). It causes a typical triad of diffuse corneal opacities, target cell hemolytic anemia, and proteinuria with renal failure. {ECO:0000269|PubMed:11423760, ECO:0000269|PubMed:12957688, ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:16051254, ECO:0000269|PubMed:16216249, ECO:0000269|PubMed:1681161, ECO:0000269|PubMed:1859405, ECO:0000269|PubMed:2370048, ECO:0000269|PubMed:7607641, ECO:0000269|PubMed:7711728, ECO:0000269|PubMed:8318557, ECO:0000269|PubMed:8432868, ECO:0000269|PubMed:8807342, ECO:0000269|PubMed:9007616, ECO:0000269|PubMed:9741700}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Fish-eye disease (FED) [MIM:136120]: A disorder of lipoprotein metabolism due to partial lecithin-cholesterol acyltransferase deficiency that affects only alpha-LCAT activity. FED is characterized by low plasma HDL and corneal opacities due to accumulation of cholesterol deposits in the cornea ('fish-eye'). {ECO:0000269|PubMed:1516702, ECO:0000269|PubMed:1571050, ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:1737840, ECO:0000269|PubMed:21901787, ECO:0000269|PubMed:8620346, ECO:0000269|PubMed:9261271}. The disease is caused by variants affecting the gene represented in this entry.

DB04083

NA

EC 4.4.1.11

3D-structure; Direct protein sequencing; Lyase; Pyridoxal phosphate

A,C

85234.4

796

0.07

37.1

6.21

-11.34

-5.96

ITGB3

Homo sapiens (Human)

GPIIIa; GP3A; CD61

Integrin beta chain family

Integrin

Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. Fibrinogen binding enhances SELP expression in activated platelets. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling. ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling. ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling. ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling. ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor.

Glanzmann thrombasthenia 2 (GT2) [MIM:619267]: A form of Glanzmann thrombasthenia, a disorder characterized by failure of platelet aggregation, absent or diminished clot retraction, and mucocutaneous bleeding of mild-to-moderate severity. Glanzmann thrombasthenia has been classified into clinical types I and II. In type I, platelets show absence of glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express glycoprotein IIb-IIIa complexes at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. {ECO:0000269|PubMed:10233432, ECO:0000269|PubMed:11588040, ECO:0000269|PubMed:11897046, ECO:0000269|PubMed:12083483, ECO:0000269|PubMed:12353082, ECO:0000269|PubMed:1371279, ECO:0000269|PubMed:1438206, ECO:0000269|PubMed:15583747, ECO:0000269|PubMed:15634267, ECO:0000269|PubMed:15748237, ECO:0000269|PubMed:1602006, ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:2392682, ECO:0000269|PubMed:29084015, ECO:0000269|PubMed:8781422, ECO:0000269|PubMed:9215749, ECO:0000269|PubMed:9376589, ECO:0000269|PubMed:9684783, ECO:0000269|PubMed:9790984}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Bleeding disorder, platelet-type, 24 (BDPLT24) [MIM:619271]: An autosomal dominant disorder of platelet production characterized by congenital macrothrombocytopenia and platelet anisocytosis. Affected individuals may have no or only mildly increased bleeding tendency. {ECO:0000269|PubMed:18065693, ECO:0000269|PubMed:29380037}. The disease is caused by variants affecting the gene represented in this entry.

DB00054; DB00098; DB00063; DB13949; DB15598; DB06472; DB04863; DB00451; DB05787; DB02709; DB14520; DB00775

P78423; P21333; P08514; P08514-1; P06756; P05106; P18031; Q9Y490; P05094; F5HB81; Q62101; P05480-2; P26039; P54939; P06935

NA

3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane; Cell projection; Direct protein sequencing; Disease variant; Disulfide bond; EGF-like domain; Glycoprotein; Host cell receptor for virus entry; Host-virus interaction; Integrin; Magnesium; Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane; Proteomics identification; Receptor; Reference proteome; Repeat; Signal; Synapse; Transmembrane; Transmembrane helix

A,B

100489

919

0.09

41.28

5.03

-27.15

-5.96

CUL4A/CUL4B-DDB1-CRBN

Homo sapiens (Human)

NA

Cullin family

NA

NA

Orotic aciduria 1 (ORAC1) [MIM:258900]: A disorder of pyrimidine metabolism resulting in megaloblastic anemia and orotic acid crystalluria that is frequently associated with some degree of physical and intellectual disability. A minority of cases have additional features, particularly congenital malformations and immune deficiencies. {ECO:0000269|PubMed:9042911}. The disease is caused by variants affecting the gene represented in this entry.

NA

P54253; Q86VP6; Q16531; Q92466; P08238; O94888; P55072

NA

3D-structure; Alternative splicing; Biological rhythms; DNA damage; DNA repair; Host-virus interaction; Isopeptide bond; Phosphoprotein; Proteomics identification; Reference proteome; Ubl conjugation; Ubl conjugation pathway

B

42669.7

368

0.1

44.94

8.72

6.58

-5.96

SERPINA1

Homo sapiens (Human)

SERPINA1; PRO0684/PRO2209; Alpha1-proteinase; Alpha-1-antiproteinase; Alpha-1 protease inhibitor

Serpin family

Serpin protein

Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin.

Alpha-1-antitrypsin deficiency (A1ATD) [MIM:613490]: A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age. {ECO:0000269|PubMed:1905728, ECO:0000269|PubMed:2227940, ECO:0000269|PubMed:2390072}. The disease is caused by variants affecting the gene represented in this entry.

DB01998; DB09130; DB00080; DB03345; DB14007; DB05961; DB05481; DB01593; DB14487; DB14533; DB14548

Q9Y282; Q8N7X4; P01009; P43307; O15393; P00772; P71213; P00760

NA

3D-structure; Acute phase; Alternative splicing; Blood coagulation; Direct protein sequencing; Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Hemostasis; Phosphoprotein; Protease inhibitor; Proteomics identification; Reference proteome; Secreted; Serine protease inhibitor; Signal

A

41542.2

370

0.09

30.24

5.56

-9.66

-5.97

PNMT

Homo sapiens (Human)

PNMTase; PENT; Noradrenaline N-methyltransferase

Class I-like SAM-binding methyltransferase superfamily, NNMT/PNMT/TEMT family

NA

Converts noradrenaline to adrenaline.

A chromosomal aberration involving TRIM24/TIF1 is found in papillary thyroid carcinomas (PTCs). Translocation t(7;10)(q32;q11) with RET. The translocation generates the TRIM24/RET (PTC6) oncogene. {ECO:0000269|PubMed:10439047}.

DB08129; DB08128; DB07739; DB07798; DB07747; DB03468; DB08550; DB03824; DB04273; DB07906; DB07597; DB09571; DB00968; DB08631; DB01752; DB08654

Q9P2G9-2; Q8TBB1

EC 2.1.1.28

3D-structure; Catecholamine biosynthesis; Direct protein sequencing; Methyltransferase; Phosphoprotein; Proteomics identification; Reference proteome; S-adenosyl-L-methionine; Transferase

A

29198.9

264

0.09

54.33

5.91

-3.69

-5.96

MycB pknB

Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

pknB; Serine/threonineprotein kinase PknB

Protein kinase superfamily, Ser/Thr protein kinase family

NA

Key component of a signal transduction pathway that regulates cell growth and cell division via phosphorylation of target proteins such as GarA, GlmU, PapA5, PbpA, FhaB (Rv0019c), FhaA(Rv0020c), MviN, PstP, EmbR, Rv1422, Rv1747 and RseA. Shows a strong preference for Thr versus Ser as the phosphoacceptor.

Immunodeficiency 67 (IMD67) [MIM:607676]: An autosomal recessive primary immunodeficiency characterized by recurrent, life-threatening systemic and invasive bacterial infections beginning in infancy or early childhood. {ECO:0000269|PubMed:12637671, ECO:0000269|PubMed:12925671, ECO:0000269|PubMed:16950813, ECO:0000269|PubMed:17878374, ECO:0000269|PubMed:19663824, ECO:0000269|PubMed:21057262, ECO:0000269|PubMed:24316379}. The disease is caused by variants affecting the gene represented in this entry.

DB02930; DB03909; DB12010

P71590; P9WJA9; P9WI81

NA

3D-structure; Acetylation; ATP-binding; Cell membrane; Direct protein sequencing; Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase; Transmembrane; Transmembrane helix; Virulence

A

28718.1

263

0.06

32.29

5.44

-9.7

-5.96

Bact metB

Escherichia coli (strain K12)

metB; O-succinylhomoserine (Thiol)-lyase; CGS

Trans-sulfuration enzymes family

Alkyl aryl transferase

Catalyzes the formation of L-cystathionine from O- succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma- replacement reaction. In the absence of thiol, catalyzes gamma- elimination to form 2-oxobutanoate, succinate and ammonia.

Congenital disorder of glycosylation 2A (CDG2A) [MIM:212066]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:11228641, ECO:0000269|PubMed:8808595}. The disease is caused by variants affecting the gene represented in this entry.

DB04083

NA

EC 2.5.1.48

3D-structure; Amino-acid biosynthesis; Cytoplasm; Direct protein sequencing; Methionine biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase

A,C

82360.8

767

0.06

34.34

5.9

-12.3

-5.95

Hepatitis A virus HAVCR2

Homo sapiens (Human)

TIMD3; TIMD-3; TIM3; TIM-3; T-cell membrane protein 3; T-cell immunoglobulin mucin receptor 3; T-cell immunoglobulin and mucin domain-containing protein 3; HAVcr-2; HAVCR2; CD366

Immunoglobulin superfamily, TIM family

Immunoglobulin

Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand. Regulates macrophage activation. Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. In CD8+ cells attenuates TCR-induced signaling, specifically by blocking NF-kappaB and NFAT promoter activities resulting in the loss of IL-2 secretion. The function may implicate its association with LCK proposed to impair phosphorylation of TCR subunits, and/or LGALS9-dependent recruitment of PTPRC to the immunological synapse. In contrast, shown to activate TCR-induced signaling in T-cells probably implicating ZAP70, LCP2, LCK and FYN. Expressed on Treg cells can inhibit Th17 cell responses. Receptor for LGALS9. Binding to LGALS9 is believed to result in suppression of T-cell responses; the resulting apoptosis of antigen-specific cells may implicate HAVCR2 phosphorylation and disruption of its association with BAG6. Binding to LGALS9 is proposed to be involved in innate immune response to intracellular pathogens. Expressed on Th1 cells interacts with LGALS9 expressed on Mycobacterium tuberculosis-infected macrophages to stimulate antibactericidal activity including IL-1 beta secretion and to restrict intracellular bacterial growth. However, the function as receptor for LGALS9 has been challenged. Also reported to enhance CD8+ T-cell responses to an acute infection such as by Listeria monocytogenes. Receptor for phosphatidylserine (PtSer); PtSer-binding is calcium-dependent. May recognize PtSer on apoptotic cells leading to their phagocytosis. Mediates the engulfment of apoptotic cells by dendritic cells. Expressed on T-cells, promotes conjugation but not engulfment of apoptotic cells. Expressed on dendritic cells (DCs) positively regulates innate immune response and in synergy with Toll-like receptors promotes secretion of TNF-alpha. In tumor-imfiltrating DCs suppresses nucleic acid-mediated innate immune repsonse by interaction with HMGB1 and interfering with nucleic acid-sensing and trafficking of nucleid acids to endosomes. Expressed on natural killer (NK) cells acts as a coreceptor to enhance IFN-gamma production in response to LGALS9. In contrast, shown to suppress NK cell-mediated cytotoxicity. Negatively regulates NK cell function in LPS-induced endotoxic shock. Cell surface receptor implicated in modulating innate and adaptive immune responses.

May be involved in T-cell exhaustion associated with chronic viral infections such as with human immunodeficiency virus (HIV) and hepatitic C virus (HCV). {ECO:0000269|PubMed:19001139, ECO:0000269|PubMed:19587053}.; DISEASE: T-cell lymphoma, subcutaneous panniculitis-like (SPTCL) [MIM:618398]: An uncommon form of T-cell non-Hodgkin lymphoma, in which cytotoxic CD8+ T-cells infiltrate subcutaneous adipose tissue, and rimming adipocytes in a lace-like pattern. Affected individuals typically present with multiple subcutaneous nodules, systemic B-cell symptoms, and, in a subset of cases, autoimmune disorders, most commonly systemic lupus erythematosus. A subset of patients develop hemophagocytic lymphohistiocytosis. SPTCL transmission pattern is consistent with autosomal recessive inheritance with incomplete penetrance. {ECO:0000269|PubMed:30374066, ECO:0000269|PubMed:30792187, ECO:0000269|Ref.2}. Disease susceptibility is associated with variants affecting the gene represented in this entry.

NA

P13688; Q96IW7; Q8N2M4

NA

3D-structure; Adaptive immunity; Alternative splicing; Cell junction; Cell membrane; Disease variant; Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Inflammatory response; Innate immunity; Membrane; Metal-binding; Phosphoprotein; Proteomics identification; Reference proteome; Signal; Transmembrane; Transmembrane helix

A

12286.9

109

0.12

26.55

5.04

-2.58

-5.96

KDM4C

Homo sapiens (Human)

KIAA0780; Jumonji domain-containing protein 2C; JmjC domain-containing histone demethylation protein 3C; JMJD2C; JHDM3C; Gene amplified in squamous cell carcinoma 1 protein; GASC1; GASC-1 protein

JHDM3 histone demethylase family

Paired donor oxygen oxidoreductase

Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code.

Renal cell carcinoma (RCC) [MIM:144700]: Renal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype. {ECO:0000269|PubMed:20054297, ECO:0000269|PubMed:23622243, ECO:0000269|PubMed:23792563, ECO:0000269|PubMed:25728682}. The disease may be caused by variants affecting the gene represented in this entry. Defects of SETD2 are associated with loss of DNA methylation at non-promoter regions (PubMed:23792563). SETD2 defects lead to aberrant and reduced nucleosome compaction and chromatin association of key replication proteins, such as MCM7 and DNA polymerase delta, leading to hinder replication fork progression and prevent loading of RAD51 homologous recombination repair factor at DNA breaks (PubMed:25728682). {ECO:0000269|PubMed:23792563, ECO:0000269|PubMed:25728682}.; DISEASE: Luscan-Lumish syndrome (LLS) [MIM:616831]: An autosomal dominant syndrome with a variable phenotype. Clinical features include macrocephaly, distinctive facial appearance, postnatal overgrowth, various degrees of learning difficulties, autism spectrum disorder, and intellectual disability. {ECO:0000269|PubMed:23160955, ECO:0000269|PubMed:24852293, ECO:0000269|PubMed:26084711, ECO:0000269|PubMed:27317772}. The disease may be caused by variants affecting the gene represented in this entry.; DISEASE: Leukemia, acute lymphoblastic (ALL) [MIM:613065]: A subtype of acute leukemia, a cancer of the white blood cells. ALL is a malignant disease of bone marrow and the most common malignancy diagnosed in children. The malignant cells are lymphoid precursor cells (lymphoblasts) that are arrested in an early stage of development. The lymphoblasts replace the normal marrow elements, resulting in a marked decrease in the production of normal blood cells. Consequently, anemia, thrombocytopenia, and neutropenia occur to varying degrees. The lymphoblasts also proliferate in organs other than the marrow, particularly the liver, spleen, and lymphnodes. {ECO:0000269|PubMed:24509477, ECO:0000269|PubMed:24662245}. The disease may be caused by variants affecting distinct genetic loci, including the gene represented in this entry.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:16314571, ECO:0000269|PubMed:24509477}. The disease may be caused by variants affecting distinct genetic loci, including the gene represented in this entry.; DISEASE: Intellectual developmental disorder, autosomal dominant 70 (MRD70) [MIM:620157]: An autosomal dominant disorder characterized by mild global developmental delay, moderately impaired intellectual disability with speech difficulties, and behavioral abnormalities. {ECO:0000269|PubMed:32710489}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Rabin-Pappas syndrome (RAPAS) [MIM:620155]: An autosomal dominant neurodevelopmental disorder characterized by severely impaired global development, intellectual disability, microcephaly, facial dysmorphism, and variable congenital anomalies affecting the skeletal, genitourinary, cardiac, and other organ systems. {ECO:0000269|PubMed:32710489}. The disease is caused by variants affecting the gene represented in this entry.

NA

NA

EC 1.14.11.-

3D-structure; Alternative splicing; Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Proteomics identification; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger

A

39355.6

338

0.14

38.34

8.04

2.41

-5.96

MRM2

Homo sapiens (Human)

rRNA methyltransferase 2, mitochondrial; Protein ftsJ homolog 2; 16S rRNA [Um1369] 2'-O-methyltransferase; 16S rRNA (uridine(1369)-2'-O)-methyltransferase

Class I-like SAM-binding methyltransferase superfamily, RNA methyltransferase RlmE family

Methyltransferase

S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.

Mitochondrial DNA depletion syndrome 17 (MTDPS17) [MIM:618567]: An autosomal recessive mitochondrial disorder characterized by childhood onset of rapidly progressive encephalopathy, stroke-like episodes, lactic acidosis, hypocitrullinemia, multiple defects of oxidative phosphorylation, mitochondrial complex I and IV deficiency, and reduced mtDNA copy number. {ECO:0000269|PubMed:28973171}. The disease may be caused by variants affecting the gene represented in this entry.

NA

NA

EC 2.1.1.-

3D-structure; Disease variant; Methyltransferase; Mitochondrion; Primary mitochondrial disease; Proteomics identification; Reference proteome; rRNA processing; S-adenosyl-L-methionine; Transferase; Transit peptide

A

20008.8

181

0.07

53.22

8.43

1.79

-5.97

ITGB3

Homo sapiens (Human)

NA

GP3A

Integrin beta chain family

Cell adhesion

Cell adhesion molecule binding.Coreceptor activity.Enzyme binding.Extracellular matrix binding.Fibronectin binding.Identical protein binding.Platelet-derived growth factor receptor binding.Protease binding.Protein disulfide isomerase activity.Vascular endothelial growth factor receptor 2 binding.Virus receptor activity.

Glanzmann thrombasthenia 2 (GT2) [MIM:619267]: A form of Glanzmann thrombasthenia, a disorder characterized by failure of platelet aggregation, absent or diminished clot retraction, and mucocutaneous bleeding of mild-to-moderate severity. Glanzmann thrombasthenia has been classified into clinical types I and II. In type I, platelets show absence of glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express glycoprotein IIb-IIIa complexes at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. {ECO:0000269|PubMed:10233432, ECO:0000269|PubMed:11588040, ECO:0000269|PubMed:11897046, ECO:0000269|PubMed:12083483, ECO:0000269|PubMed:12353082, ECO:0000269|PubMed:1371279, ECO:0000269|PubMed:1438206, ECO:0000269|PubMed:15583747, ECO:0000269|PubMed:15634267, ECO:0000269|PubMed:15748237, ECO:0000269|PubMed:1602006, ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:2392682, ECO:0000269|PubMed:29084015, ECO:0000269|PubMed:8781422, ECO:0000269|PubMed:9215749, ECO:0000269|PubMed:9376589, ECO:0000269|PubMed:9684783, ECO:0000269|PubMed:9790984}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Bleeding disorder, platelet-type, 24 (BDPLT24) [MIM:619271]: An autosomal dominant disorder of platelet production characterized by congenital macrothrombocytopenia and platelet anisocytosis. Affected individuals may have no or only mildly increased bleeding tendency. {ECO:0000269|PubMed:18065693, ECO:0000269|PubMed:29380037}. The disease is caused by variants affecting the gene represented in this entry.

DB00054; DB00098; DB00063; DB13949; DB15598; DB06472; DB04863; DB00451; DB05787; DB02709; DB14520; DB00775

P78423; P21333; P08514; P08514-1; P06756; P05106; P18031; Q9Y490; P05094; F5HB81; Q62101; P05480-2; P26039; P54939; P06935

NA

3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane; Cell projection; Direct protein sequencing; Disease variant; Disulfide bond; EGF-like domain; Glycoprotein; Host cell receptor for virus entry; Host-virus interaction; Integrin; Magnesium; Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane; Proteomics identification; Receptor; Reference proteome; Repeat; Signal; Synapse; Transmembrane; Transmembrane helix

B,D

70443.1

646

0.11

41.21

5.02

-21.12

-5.95

CYP2C8

Homo sapiens (Human)

NA

NA

Cytochrome P450 family

Oxidoreductase

Arachidonic acid epoxygenase activity.Aromatase activity.Caffeine oxidase activity.Estrogen 16-alpha-hydroxylase activity.Heme binding.Iron ion binding.Monooxygenase activity.Oxygen binding.

A chromosomal aberration involving BCL2 has been found in chronic lymphatic leukemia. Translocation t(14;18)(q32;q21) with immunoglobulin gene regions. BCL2 mutations found in non-Hodgkin lymphomas carrying the chromosomal translocation could be attributed to the Ig somatic hypermutation mechanism resulting in nucleotide transitions. {ECO:0000269|PubMed:2875799, ECO:0000269|PubMed:3285301}.

DB08607; DB08496; DB14055; DB12001; DB05812; DB15568; DB00918; DB12015; DB01424; DB01118; DB00321; DB00381; DB00613; DB01060; DB17449; DB01217; DB01435; DB11901; DB06605; DB00714; DB01072; DB01076; DB11995; DB00972; DB08822; DB12781; DB13997; DB05015; DB16703; DB06770; DB05229; DB00443; DB12236; DB00307; DB01393; DB13746; DB16536; DB06616; DB12267; DB12151; DB01194; DB01222; DB00921; DB06772; DB08875; DB00201; DB13919; DB00796; DB09061; DB08502; DB00564; DB00482; DB06119; DB00439; DB00608; DB00169; DB09201; DB00501; DB00604; DB12499; DB00349; DB00845; DB00758; DB00257; DB00363; DB00907; DB01394; DB05219; DB00531; DB08912; DB11682; DB00250; DB09183; DB01609; DB01234; DB14649; DB09213; DB00829; DB00586; DB00255; DB00343; DB01184; DB00625; DB11979; DB15444; DB06210; DB13874; DB11718; DB08899; DB00530; DB00783; DB13952; DB13953; DB13954; DB13955; DB13956; DB00402; DB00977; DB14766; DB00973; DB12466; DB04854; DB01023; DB01039; DB16165; DB00544; DB13867; DB08906; DB00588; DB01095; DB11679; DB01241; DB01645; DB11978; DB01218; DB00741; DB14538; DB14539; DB14540; DB14541; DB14542; DB14543; DB14545; DB14544; DB01611; DB12471; DB01050; DB09054; DB01181; DB00619; DB16200; DB01029; DB11633; DB06636; DB00951; DB11757; DB14568; DB09570; DB01221; DB06738; DB01026; DB01009; DB00465; DB00448; DB01259; DB09078; DB12070; DB05667; DB08918; DB00451; DB04725; DB00281; DB17083; DB01583; DB09198; DB06448; DB00836; DB00455; DB12130; DB00678; DB00227; DB09280; DB15935; DB06077; DB08932; DB14921; DB14009; DB00603; DB00784; DB00814; DB00170; DB00532; DB01357; DB00333; DB09241; DB00959; DB00916; DB01110; DB06595; DB00834; DB16236; DB11763; DB00764; DB14512; DB00471; DB00295; DB06510; DB00688; DB01024; DB00486; DB00788; DB09199; DB00622; DB00184; DB01115; DB04868; DB06712; DB12005; DB06670; DB09080; DB16267; DB12513; DB09296; DB00338; DB11632; DB01062; DB12612; DB01229; DB03796; DB05467; DB00617; DB06589; DB08922; DB00850; DB00780; DB01174; DB00946; DB00252; DB01132; DB00554; DB17472; DB08860; DB08901; DB15822; DB14631; DB00635; DB01032; DB00818; DB00205; DB04216; DB00908; DB00468; DB01129; DB00481; DB08896; DB11853; DB14761; DB00912; DB16826; DB00615; DB01045; DB11753; DB01201; DB01220; DB08864; DB08931; DB14840; DB14924; DB00503; DB09200; DB00533; DB00412; DB04847; DB12332; DB00938; DB12543; DB01232; DB00418; DB01037; DB11362; DB15685; DB11689; DB06739; DB00641; DB01261; DB00398; DB15569; DB00421; DB09118; DB00359; DB06729; DB01138; DB00675; DB00799; DB12020; DB09256; DB01079; DB12095; DB15133; DB00857; DB00342; DB08880; DB00624; DB13943; DB13944; DB13946; DB11712; DB00208; DB06137; DB01124; DB01685; DB00214; DB08911; DB00374; DB00755; DB00897; DB12245; DB12808; DB00347; DB00440; DB00197; DB13179; DB11652; DB15328; DB12255; DB15114; DB00862; DB11613; DB08881; DB00661; DB08828; DB09068; DB12026; DB00682; DB00549; DB01198

P13473-2; O75400-2; Q9Y371

1.14.14.1

3D-structure; Alternative splicing; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Phosphoprotein; Proteomics identification; Reference proteome; Steroid metabolism

A

52511

463

0.1

37.03

8.6

6.74

-5.94

PNP

Homo sapiens (Human)

PNP; Inosine phosphorylase

PNP/MTAP phosphorylase family

Pentosyltransferase

The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.

Purine nucleoside phosphorylase deficiency (PNPD) [MIM:613179]: A disorder that interrupts both the catabolism of inosine into hypoxanthine and guanosine into guanine, and leads to the accumulation of guanosine, inosine, and their deoxified by-products. The main clinical presentation is recurrent infections due to severe T-cell immunodeficiency. Some patients also have neurologic impairment. {ECO:0000269|PubMed:1384322, ECO:0000269|PubMed:3029074, ECO:0000269|PubMed:8931706}. The disease is caused by variants affecting the gene represented in this entry.

DB03881; DB03551; DB02222; DB02391; DB03609; DB01667; DB04260; DB02796; DB04753; DB00640; DB00242; DB00900; DB06185; DB02377; DB02857; DB04754; DB04757; DB04076; DB02230; DB04335; DB02568; DB03101

P05067; Q9UQM7; O14576-2; P06241; P14136; Q92993-2; Q9BXM7; P00491; P17612; P63000; Q92673; Q15583

EC 2.4.2.1

3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Disease variant; Glycosyltransferase; Phosphoprotein; Proteomics identification; Purine salvage; Reference proteome; Transferase

A,B,C

31849.2

288

0.1

34.77

6.42

-1.63

-5.94

CYP11A1

Homo sapiens (Human)

P450(scc); Cytochrome P450(scc); Cytochrome P450 11A1; Cholesterol side-chain cleavage enzyme, mitochondrial; CYPXIA1; CYP11A

Adrenodoxin/putidaredoxin family

Paired donor oxygen oxidoreductase

Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone, the precursor of most steroid hormones.

Leukocyte adhesion deficiency 1 (LAD1) [MIM:116920]: LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions. {ECO:0000269|PubMed:1346613, ECO:0000269|PubMed:1347532, ECO:0000269|PubMed:1352501, ECO:0000269|PubMed:1590804, ECO:0000269|PubMed:1694220, ECO:0000269|PubMed:1968911, ECO:0000269|PubMed:20529581, ECO:0000269|PubMed:20549317, ECO:0000269|PubMed:7509236, ECO:0000269|PubMed:7686755, ECO:0000269|PubMed:9884339}. The disease is caused by variants affecting the gene represented in this entry.

DB00648

NA

EC 1.14.15.6

2Fe-2S; 3D-structure; Acetylation; Cholesterol metabolism; Electron transport; Iron; Iron-sulfur; Lipid metabolism; Metal-binding; Mitochondrion; Phosphoprotein; Proteomics identification; Reference proteome; Steroid metabolism; Steroidogenesis; Sterol metabolism; Transit peptide; Transport

C,D

54754.5

470

0.13

33.2

8.16

2.32

-5.94

folC

Escherichia coli (strain K12)

NA

dedC;JW2312;b2315

Folylpolyglutamate synthase family

Synthase

ATP binding.Dihydrofolate synthase activity.Metal ion binding.Tetrahydrofolylpolyglutamate synthase activity.

Complement hyperactivation, angiopathic thrombosis, and protein-losing enteropathy (CHAPLE) [MIM:226300]: An autosomal recessive disease characterized by abdominal pain and diarrhea, primary intestinal lymphangiectasia, edema due to hypoproteinemia, malabsorption, and less frequently, bowel inflammation, recurrent infections, and angiopathic thromboembolic disease. Patients' T lymphocytes show increased complement activation causing surface deposition of complement and the generation of soluble C5a. {ECO:0000269|PubMed:28657829, ECO:0000269|PubMed:28657861}. The disease is caused by variants affecting the gene represented in this entry. CHAPLE is caused by biallelic mutations in the CD55 gene.

DB02437; DB03830

NA

6.3.2.12; 6.3.2.17

3D-structure; ATP-binding; Folate biosynthesis; Ligase; Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism; Reference proteome

A

44392.8

414

0.07

29.47

5.2

-15.5

-5.94

nadE

Bacillus subtilis (strain 168)

NA

outB;BSU03130

NAD synthetase family

Ligase

ATP binding.Metal ion binding.NAD+ synthase (glutamine-hydrolyzing) activity.NAD+ synthase activity.

Leukodystrophy, hypomyelinating, 15 (HLD15) [MIM:617951]: An autosomal recessive disorder characterized by hypomyelinating leukodystrophy with thinning of the corpus callosum. Clinical features include motor and cognitive impairment appearing in the first or second decade of life, dystonia, ataxia, spasticity, and dysphagia. Most patients develop severe optic atrophy, and some have hearing loss. {ECO:0000269|PubMed:29576217}. The disease may be caused by variants affecting the gene represented in this entry.

DB02596; DB04099; DB00798

NA

6.3.1.5

3D-structure; ATP-binding; Direct protein sequencing; Ligase; Magnesium; Metal-binding; NAD; Nucleotide-binding; Phosphoprotein; Reference proteome; Sporulation; Stress response

A,B

60509.3

542

0.08

31.96

5.07

-19.73

-5.95

penA

Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

NA

spr1517;pbp2b

Transpeptidase family

Peptide binding protein

Penicillin binding.

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.

DB01163; DB00415; DB08795; DB01140; DB00456; DB01066; DB00493; DB01331; DB01212; DB00567; DB03313; DB00485; DB00739; DB01603; DB00607; DB00713; DB00319

NA

NA

3D-structure; Antibiotic resistance; Cell membrane; Cell shape; Cell wall biogenesis/degradation; Membrane; Peptidoglycan synthesis; Reference proteome; Transmembrane; Transmembrane helix

A,B,C

65444.4

607

0.08

30.15

4.95

-20.68

-5.95