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https://en.wikipedia.org/wiki/EIF3C | Eukaryotic translation initiation factor 3 subunit C (eIF3c) is a protein that in humans is encoded by the EIF3C gene.
Interactions
EIF3C has been shown to interact with EIF3G and EIF3A.
See also
Eukaryotic initiation factor 3 (eIF3)
References
Further reading |
https://en.wikipedia.org/wiki/EIF3H | Eukaryotic translation initiation factor 3 subunit H (eIF3h) is a protein that in humans is encoded by the EIF3H gene.
Interactions
eIF3h has been shown to interact with eIF3a.
See also
Eukaryotic initiation factor 3 (eIF3)
References
Further reading
External links |
https://en.wikipedia.org/wiki/CDC23 | Cell division cycle 23 homolog (S. cerevisiae), also known as CDC23, is a protein that, in humans, is encoded by the CDC23 gene.
Function
The CDC23 protein shares strong similarity with Saccharomyces cerevisiae Cdc23, a protein essential for cell cycle progression through the G2/M transition. This protein is a component of anaphase-promoting complex (APC), which is composed of eight protein subunits and highly conserved in eukaryotic cells. APC catalyzes the formation of cyclin B-ubiquitin conjugate that is responsible for the ubiquitin-mediated proteolysis of B-type cyclins. This protein and 3 other members of the APC complex contain the TPR (tetratricopeptide repeat), a protein domain important for protein-protein interaction.
Interactions
CDC23 has been shown to interact with CDC27.
References
External links
Further reading |
https://en.wikipedia.org/wiki/ADAM19 | ADAM19 (A Disintegrin And Metalloproteinase 19, MADDAM, meltrin beta), is a human gene.
Function
This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. This member is a type I transmembrane protein and serves as a marker for dendritic cell differentiation. It has also been demonstrated to be an active metalloproteinase, which may be involved in normal physiological and pathological processes such as cells migration, cell adhesion, cell-cell and cell-matrix interactions, and signal transduction. Alternative splicing results in two transcript variants.
Interactions
ADAM19 has been shown to interact with ABI2.
References
External links
Further reading
Proteases
Human proteins
EC 3.4.24 |
https://en.wikipedia.org/wiki/SYNGAP1 | Synaptic Ras GTPase-activating protein 1, also known as synaptic Ras-GAP 1 or SYNGAP1, is a protein that in humans is encoded by the SYNGAP1 gene. SYNGAP1 is a ras GTPase-activating protein that is critical for the development of cognition and proper synapse function. Mutations in humans can cause intellectual disability, epilepsy, autism and sensory processing deficits.
Function
SynGAP1 is a complex protein with several functions that may be regulated temporally via complex isoforms. A well-documented function of SynGAP1 involves NMDA receptor-mediated synaptic plasticity and membrane insertion of AMPA receptors through the suppression of upstream signaling pathways. However, SynGAP1 has also been shown to function cooperatively with Unc51.1 in axon formation. One way SynGAP1 affects these processes is through the MAP kinase signaling pathway by attenuation of Ras signalling. However, alternative splicing and multiple translational start sites have been shown to cause opposing effects, illustrating the importance of multiple functional domains that reside within the c- and n-termini. For example, the expression of an α1 or α2 c-terminal variant of SynGAP1 will either increase or decrease synaptic strength, respectively. Overall, SynGAP1 is essential for development and survival, which is evident as knockout mice die perinatally.
Dendritic spine development and maturation
SynGAP1 is shown to localize at the postsynaptic density on the dendritic spines of excitatory synap |
https://en.wikipedia.org/wiki/APPBP1 | NEDD8-activating enzyme E1 regulatory subunit is a protein that in humans is encoded by the NAE1 gene.
Function
The protein encoded by this gene binds to the beta-amyloid precursor protein. Beta-amyloid precursor protein is a cell surface protein with signal-transducing properties, and it is thought to play a role in the pathogenesis of Alzheimer's disease. In addition, the encoded protein can form a heterodimer with UBE1C and bind and activate NEDD8, a ubiquitin-like protein. This protein is required for cell cycle progression through the S/M checkpoint. Three transcript variants encoding different isoforms have been found for this gene.
APPBP1 (Amyloid Precursor Protein-Binding Protein 1) binds to the Amyloid Precursor Protein (APP) carboxy terminal domain. APPBP1 is a multi-functional protein with activities in neuronal tissues. APPBP1 also bonds with UBA3 (ubiquitin-like protein-activating enzyme 3) to form the NEDD8 activating enzyme (NAE). Activated NEDD8 is an enzyme that regulates multiple cellular pathways.
History
APPBP1 was first cloned and identified by its interaction with the C-terminus of beta-amyloid protein precursor (precursor to beta-amyloid present in Alzheimer's disease) in 1996. APPBP1 was first studied for its potential neuronal effects, and neuronal effects continue to be further investigated (e.g. references).
Role in NEDD8 activation
APPBP1 can bind to UBA3 to form the NEDD8 activating enzyme (NAE) (homologous to the ubiquitin-activating |
https://en.wikipedia.org/wiki/SKAP2 | Src kinase-associated phosphoprotein 2 is an enzyme that in humans is encoded by the SKAP2 gene.
Function
The protein encoded by this gene belongs to the src family kinases. This protein is similar to the src kinase associated phosphoprotein 1. It is an adaptor protein that is thought to play an essential role in the src signaling pathway in various cells, but particularly specific in macrophages. It inhibits PTK2B/RAFTK activity and regulates alpha-synuclein phosphorylation. It interacts with Signal-regulatory protein alpha and directs integrin-activated cytoskeletal reorganization in macrophages.
References
Further reading |
https://en.wikipedia.org/wiki/HM13 | Minor histocompatibility antigen H13 is a protein that in humans is encoded by the HM13 gene.
Function
The minor histocompatibility antigen 13 is a nonamer peptide that originates from a protein encoded by the H13 gene. The peptide is generated by the cytosol by the proteasome, enters the endoplasmic reticulum (ER) lumen by the transporter associated with antigen processing (TAP) and is presented on the cell surface on H2-Db major histocompatibility antigen I (MHC I) molecules. The alloreactivity, which leads to transplant rejection in mice, is conferred by Val/Ile polymorphism in the ‘SSV(V/I)GVWYL’ peptide. The orthologue gene in humans is called HM13. If a related polymorphism exists, and if the HM13 serves as a Minor histocompatibility antigen, however, remains to be addressed.
The protein encoded by the M13/HM13 gene is the signal peptide peptidase (SPP), an ER-resident intramembrane protease.
SPP localizes to the endoplasmic reticulum, catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. This activity is required to generate signal sequence-derived human lymphocyte antigen-E epitopes that are recognized by the immune system, and to process hepatitis C virus core protein. The encoded protein is an integral membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases. Multiple transcript variants encoding several different isoforms have been found for this gene.
References
Furth |
https://en.wikipedia.org/wiki/ITM2C | Integral membrane protein 2C is a protein that in humans is encoded by the ITM2C gene.
References
Further reading |
https://en.wikipedia.org/wiki/RAB1B | Ras-related protein Rab-1B is a protein that in humans is encoded by the RAB1B gene.
Interactions
RAB1B has been shown to interact with GOLGA2.
References
Further reading |
https://en.wikipedia.org/wiki/SYVN1 | E3 ubiquitin-protein ligase synoviolin is an enzyme that in humans is encoded by the SYVN1 gene.
Function
This gene encodes a protein involved in endoplasmic reticulum (ER)-associated degradation. The encoded protein removes unfolded proteins, accumulated during ER stress, by retrograde transport to the cytosol from the ER. This protein also uses the ubiquitin-proteasome system for additional degradation of unfolded proteins. This gene and the mitochondrial ribosomal protein L49 gene use in their respective 3' UTRs some of the same genomic sequence. Sequence analysis identified two transcript variants that encode different isoforms.
References
Further reading
External links |
https://en.wikipedia.org/wiki/HOPX | Homeodomain-only protein is a protein that in humans is encoded by the HOPX gene. It is an important regulator of cardiac development and a marker of hippocampal neural stem cells.
Function
The protein encoded by this gene is a homeodomain protein that lacks certain conserved residues required for DNA binding. It was reported that choriocarcinoma cell lines and tissues failed to express this gene, which suggested the possible involvement of this gene in malignant conversion of placental trophoblasts. Studies in mice suggested that this protein may interact with serum response factor (SRF) and modulate SRF-dependent cardiac-specific gene expression and cardiac development. Multiple alternatively spliced transcript variants encoding the same protein have been observed, the full-length natures of only some have been determined.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/SCARB2 | Lysosomal integral membrane protein 2 (LIMP-2) is a protein that in humans is encoded by the SCARB2 gene. LIMP-2 is expressed in brain, heart, liver, lung and kidney, mainly in the membrane of lysosome organelles; however, in cardiac muscle, LIMP-2 is also expressed at intercalated discs. LIMP-2 in a membrane protein in lysosomes that functions to regulate lysosomal/endosomal transport. Mutations in LIMP-2 have been shown to cause Gaucher disease, myoclonic epilepsy, and action myoclonus–renal failure syndrome. Abnormal levels of LIMP-2 have also been found in patients with hypertrophic cardiomyopathy.
Structure
Human LIMP-2 has a theoretical molecular weight of 54.3 kDa and is 478 amino acids in length.
Though LIMP-2 was initially discovered in 1985 by Lewis et al. from rat liver lysosomes, LIMP-2 was cloned in 1992 by two groups, one isolated LIMP-2 from human metastatic pancreatic islet tumor cells, and one from rat liver lysosomal membranes. LIMP-2 was isolated as a protein of approximate molecular weight 85 kDa, synthesized from a precursor oform of approximately 77 kDa. The weight discrepancy between its theoretical (54.3 kDa) and observed (85 kDa) is due to the presence of 10 high mannose-type N-linked oligosaccharide chains in the human form of this protein, compared to 11 in mouse and rat. LIMP-2 has two hydrophobic regions, one near the N-terminus and one near the C-terminus, as well as a short isoleucine/leucine-rich cytoplasmic tail consisting of 20 amino acids |
https://en.wikipedia.org/wiki/CDH11 | Cadherin-11 is a protein that in humans is encoded by the CDH11 gene.
Function
This gene encodes a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Mature cadherin proteins are composed of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small, highly conserved C-terminal cytoplasmic domain. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. Expression of this particular cadherin in osteoblastic cell lines, and its upregulation during differentiation, suggests a specific function in bone development and maintenance. The mammalian CDH-11 homologues are termed calsyntenin.
Relevance to cancer
CDH11 is overexpressed in 15% of breast cancers and seems essential to tumour progression in some other cancer types.
Drug interactions
Arthritis drug celecoxib binds to CDH11.
Interactions
CDH11 has been shown to interact with CDH2.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Corneodesmosin | Corneodesmosin is a protein that in humans is encoded by the CDSN gene.
This gene encodes a protein found in corneodesmosomes, which localize to the human epidermis and other cornified squamous epithelia. During maturation of the cornified layers, the protein undergoes a series of cleavages, which are thought to be required for desquamation. The gene is located in the major histocompatibility complex (MHC) class I region on chromosome 6.
See also
Hypertrichosis simplex of the scalp
List of conditions caused by problems with junctional proteins
References
Further reading
Plakins |
https://en.wikipedia.org/wiki/UBE1C | NEDD8-activating enzyme E1 catalytic subunit is a protein that in humans is encoded by the UBA3 gene.
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E1 ubiquitin-activating enzyme family. The encoded enzyme associates with AppBp1, an amyloid beta precursor protein binding protein, to form a heterodimer, and then the enzyme complex activates NEDD8, a ubiquitin-like protein, which regulates cell division, signaling and embryogenesis. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
This enzyme contains an E2 binding domain, which resembles ubiquitin, and recruits the catalytic core of the E2 enzyme UBE2M (Ubc12) in a similar manner to that in which ubiquitin interacts with ubiquitin binding domains.
Interactions
UBE1C has been shown to interact with NEDD8, APPBP1 and UBE2M.
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human NEDD8-activating enzyme E1 catalytic subunit (UBE1C)
Protein domains |
https://en.wikipedia.org/wiki/Sperm-associated%20antigen%209 | C-jun-amino-terminal kinase-interacting protein 4 is a scaffold protein that in humans is encoded by the SPAG9 gene.
Function
Extracellular signals are transduced into cells through mitogen-activated protein kinases. The structural organization of these kinases into specific signaling domains is facilitated by scaffolding proteins involved in closely tethering different kinases so that successive phosphorylation events can occur. The protein encoded by this gene is a scaffolding protein that brings together mitogen-activated protein kinases and their transcription factor targets for the activation of specific signaling pathways. This gene which is abundantly expressed in testicular haploid germ cells encodes a protein that is recognized by sperm-agglutinating antibodies and implicated in infertility.
Clinical significance
SPAG9 is a potential biomarker for early cervical carcinoma bladder cancer, and lung cancer.
Interactions
SPAG9 has been shown to interact with MAX.
References
Further reading |
https://en.wikipedia.org/wiki/CLDN12 | Claudin-12 is a protein that in humans is encoded by the CLDN12 gene. It belongs to the group of claudins.
References
External links
Further reading |
https://en.wikipedia.org/wiki/USP8 | Ubiquitin carboxyl-terminal hydrolase 8 is an enzyme that in humans is encoded by the USP8 gene.
Interactions
USP8 has been shown to interact with RNF41 and STAM2.
References
Further reading |
https://en.wikipedia.org/wiki/N-myc-interactor | N-myc-interactor also known as N-myc and STAT interactor is a protein that in humans is encoded by the NMI gene.
Function
NMYC interactor (NMI) interacts with NMYC and CMYC (two members of the oncogene Myc family), and other transcription factors containing a Zip, HLH, or HLH-Zip motif. The NMI protein also interacts with all STATs except STAT2 and augments STAT-mediated transcription in response to cytokines IL-2 and IFN-gamma. The NMI mRNA has low expression levels in all human fetal and adult tissues tested except brain and has high expression in cancer cell line-myeloid leukemias.
Interactions
NMI (gene) has been shown to interact with BRCA1, IFI35, Myc, and STAT5A, and TUBA3C.
References
Further reading
Human proteins |
https://en.wikipedia.org/wiki/LATS1 | Large tumor suppressor kinase 1 (LATS1) is an enzyme that in humans is encoded by the LATS1 gene.
It has been associated with the Hippo signaling pathway, where it phosphorylates YAP and TAZ to inactivate their function.
The protein encoded by this gene is a putative serine/threonine kinase that localizes to the mitotic apparatus and complexes with cell cycle controller CDC2 kinase in early mitosis. The protein is phosphorylated in a cell-cycle dependent manner, with late prophase phosphorylation remaining through metaphase. The N-terminal region of the protein binds CDC2 to form a complex showing reduced histone H1 kinase activity, indicating a role as a negative regulator of CDC2/cyclin A. In addition, the C-terminal kinase domain binds to its own N-terminal region, suggesting potential negative regulation through interference with complex formation via intramolecular binding. Biochemical and genetic data suggest a role as a tumor suppressor. This is supported by studies in knockout mice showing development of soft-tissue sarcomas, ovarian stromal cell tumors and a high sensitivity to carcinogenic treatments.
Interactions
LATS1 has been shown to interact with Zyxin and Cdk1.
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/TMSB10 | Thymosin beta-10 is a protein that in humans is encoded by the TMSB10 gene. TMSB10 is a member of the beta-thymosin family of peptides.
TMSB10 plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity).
References
Further reading |
https://en.wikipedia.org/wiki/BUB3 | Mitotic checkpoint protein BUB3 is a protein that in humans is encoded by the BUB3 gene.
Bub3 is a protein involved with the regulation of the Spindle Assembly Checkpoint (SAC); though BUB3 is non-essential in yeast, it is essential in higher eukaryotes. As one of the checkpoint proteins, Bub3 delays the irreversible onset of anaphase through direction of kinetochore localization during prometaphase to achieve biorientation. In directing the kinetochore-microtubule interaction, this ensures the proper (and consequently, bioriented) attachment of the chromosomes prior to anaphase. Bub3 and its related proteins that form the Spindle Assembly Checkpoint (SAC) inhibit the action of the Anaphase Promoting Complex (APC), preventing early anaphase entry and mitotic exit; this serves as a mechanism for the fidelity of chromosomal segregation.
Function
Bub3 is a crucial component in the formation of the mitotic spindle assembly complex, which forms a complex with other important proteins. For correct segregation of the cells it is necessary for all mitotic spindles to attach correctly to the kinetochore of each chromosome. This is controlled by the mitotic spindle checkpoint complex which operates as a feedback-response. If there is a signal of a defect in the attachment, mitosis will be stopped to ensure that all chromosomes have an amphitelic binding to spindles. After the error is corrected, the cell will proceed to anaphase. The complex of proteins which regulate the cell ar |
https://en.wikipedia.org/wiki/ITGB1BP1 | Integrin beta-1-binding protein 1 is a protein that in humans is encoded by the ITGB1BP1 gene.
The cytoplasmic domains of integrins are essential for cell adhesion. The protein encoded by this gene binds to the beta1 integrin cytoplasmic domain. The interaction between this protein and beta1 integrin is highly specific. Two isoforms of this protein are derived from alternatively spliced transcripts. The shorter form of this protein does not interact with the beta1 integrin cytoplasmic domain. The longer form is a phosphoprotein and the extent of its phosphorylation is regulated by the cell-matrix interaction, suggesting an important role of this protein during integrin-dependent cell adhesion.
Interactions
ITGB1BP1 has been shown to interact with KRIT1, LRP2, CD29 and LRP1.
References
Further reading |
https://en.wikipedia.org/wiki/EFTUD2 | 116 kDa U5 small nuclear ribonucleoprotein component is a protein that in humans is encoded by the EFTUD2 gene.
Disease associations
Heterozygous loss-of-function mutations in EFTUD2 cause Mandibulofacial Dysostosis with Microcephaly (MFDM; OMIM #610536), a multiple malformation syndrome comprising progressive microcephaly (present in all affected individuals), craniofacial skeletal anomalies, cleft palate, deafness, choanal atresia, small stature, and/or cardiac and thumb anomalies.
Interactions
EFTUD2 has been shown to interact with WDR57 and PRPF8.
References
Further reading |
https://en.wikipedia.org/wiki/MATR3 | Matrin-3 is a protein that in humans is encoded by the MATR3 gene.
Function
The protein encoded by this gene is localized in the nuclear matrix. It may play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. Two transcript variants encoding the same protein have been identified for this gene.
Pathology
Mutations in the Matrin 3 gene are associated with familial amyotrophic lateral sclerosis.
References
Further reading |
https://en.wikipedia.org/wiki/RB1CC1 | RB1-inducible coiled-coil protein 1 is a protein that in humans is encoded by the RB1CC1 gene.
Interactions
RB1CC1 has been shown to interact with PTK2B, ASK1 and PTK2.
References
Further reading |
https://en.wikipedia.org/wiki/SNAP91 | Clathrin coat assembly protein AP180 is a protein that in humans is encoded by the SNAP91 gene.
References
Further reading |
https://en.wikipedia.org/wiki/MAFB%20%28gene%29 | Transcription factor MafB also known as V-maf musculoaponeurotic fibrosarcoma oncogene homolog B is a protein that in humans is encoded by the MAFB gene. This gene maps to chromosome 20q11.2-q13.1, consists of a single exon and spans around 3 kb.
Function
MafB is a basic leucine zipper (bZIP) transcription factor that plays an important role in the regulation of lineage-specific hematopoiesis. The encoded nuclear protein represses ETS1-mediated transcription of erythroid-specific genes in myeloid cells.
Clinical significance
Mutations in the murine Mafb gene are responsible for the mutant mouse Kreisler (kr) that presents an abnormal segmentation of the hindbrain and exhibit hyperactive behavior, including head tossing and running in circles. This mice dies at birth due to renal failure whereas the Mafb -/- mice dies of central apnea.
Recently, single-nucleotide polymorphisms (SNPs) near MAFB have been found associated with nonsyndromic cleft lip and palate. The GENEVA Cleft Consortium study, a genomewide association study involving 1,908 case-parent trios from Europe, the United States, China, Taiwan, Singapore, Korea, and the Philippines, first identified MAFB as being associated with cleft lip and/or palate with stronger genome-wide significance in Asian than European populations. The difference in populations could reflect variable coverage by available markers or true allelic heterogeneity. In mouse models, Mafb mRNA and protein were detected in both craniofac |
https://en.wikipedia.org/wiki/SLC23A1 | Solute carrier family 23 member 1 is a protein that in humans is encoded by the SLC23A1 gene.
Function
The absorption of vitamin C into the body and its distribution to organs requires two sodium-dependent vitamin C transporters. This gene encodes one of the two required transporters. The encoded protein is active in bulk vitamin C transport involving epithelial surfaces. Previously, this gene had an official symbol of SLC23A2.
See also
Solute carrier family
References
Further reading
Solute carrier family |
https://en.wikipedia.org/wiki/SCO2 | SCO2 cytochrome c oxidase assembly (also known as SCO2 homolog, mitochondrial and SCO cytochrome oxidase deficient homolog 2) is a protein that in humans is encoded by the SCO2 gene. The encoded protein is one of the cytochrome c oxidase (COX)(Complex IV) assembly factors. Human COX is a multimeric protein complex that requires several assembly factors. Cytochrome c oxidase (COX) catalyzes the transfer of electrons from cytochrome c to molecular oxygen, which helps to maintain the proton gradient across the inner mitochondrial membrane that is necessary for aerobic ATP production. The encoded protein is a metallochaperone that is involved in the biogenesis of cytochrome c oxidase subunit II. Mutations in this gene are associated with fatal infantile encephalocardiomyopathy and myopia 6.
Structure
The SCO2 gene is located on the q arm of chromosome 22 at position 13.33 and it spans 2,871 base pairs. The SCO2 gene produces a 15.1 kDa protein composed of 136 amino acids. The protein contains an N-terminal mitochondrial targeting presequence of 41 amino acids, and shares identity with the yeast protein in regions between glycine-102 and glycine-242 in human SCO2. SCO2 is a subunit of the enzyme Mammalian cytochrome c oxidase (COX)(Complex IV).
Function
The SCO2 gene encodes for a protein essential for the assembly and function of Mammalian cytochrome c oxidase (COX)(Complex IV) of the mitochondrial respiratory chain. SCO2 acts as a metallochaperone involved in the biogenesis |
https://en.wikipedia.org/wiki/KCNE3 | Potassium voltage-gated channel, Isk-related family, member 3 (KCNE3), also known as MinK-related peptide 2 (MiRP2) is a protein that in humans is encoded by the KCNE3 gene.
Function
Voltage-gated potassium channels (Kv) represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. KCNE3 encodes a member of the five-strong KCNE family of voltage-gated potassium (Kv) channel ancillary or β subunits.
KCNE3 is best known for modulating the KCNQ1 Kv α subunit, but it also regulates hERG, Kv2.1, Kv3.x, Kv4.x and Kv12.2 in heterologous co-expression experiments and/or in vivo.
Co-assembly with KCNE3 converts KCNQ1 from a voltage-dependent delayed rectifier K+ channel to a constitutively open K+ channel with an almost linear current/voltage (I/V) relationship. KCNQ1-KCNE3 channels have been detected in the basolateral membrane of mouse small intestinal crypts, where they provide a driving force to regulate Cl- secretion. Specific amino acids within the transmembrane segment (V72) and extracellular domain (D54 and D55) of KCNE3 are important for its control of KCNQ1 voltage dependence. D54 and D55 interact electrostatically with R237 in the S4 segment of the KCNQ1 voltage sensor, helping to stabilize S4 in the activated state, whic |
https://en.wikipedia.org/wiki/SAE2%20%28yeast%29 | SAE2 is a gene in budding yeast, coding for the protein Sae2, which is involved in DNA repair. Sae2 is a part of the homologous recombination process in response to double-strand breaks. It is best characterized in the yeast model organism Saccharomyces cerevisiae. Homologous genes in other organisms include Ctp1 in fission yeast, Com1 in plants, and CtIP in higher eukaryotes including humans.
Sae2 and its homologs have relatively long low-complexity regions in their primary sequences and appear to have large intrinsically unstructured regions. Sae2 likely forms tetramers through coiled-coil sequences. Proteins of this family are DNA-binding proteins and are involved in DNA end resection and bridging at double-strand breaks. Sae2 has been reported to have endonuclease activity, though it has no bioinformatically recognizable nuclease sequence and reports of this activity are not consistent in the literature.
References
Saccharomyces cerevisiae genes |
https://en.wikipedia.org/wiki/PTPRU | Receptor-type tyrosine-protein phosphatase PCP-2 (also known as PTP-pi, PTP lambda, hPTP-J, PTPRO and PTP psi), is an enzyme that in humans is encoded by the PTPRU gene.
Function
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracellular catalytic tyrosine phosphatase domains, and thus represents a receptor-type PTP (RPTP). The extracellular region contains a meprin-A5 antigen-PTPmu (MAM) domain, one Ig-like domain and four fibronectin type III-like repeats, and thus is a member of the type R2B RPTP family. It was cloned by many groups and given different names, including PCP-2, PTP pi, PTP lambda, hPTP-J, PTPRO, and PTP psi. Other type R2B RPTPs include PTPRM, PTPRK, and PTPRT. Analysis of the genomic structure of PCP-2 suggests that it is the most distantly related of the type R2B RPTPS.
RPTPs are able to remove phosphate moieties from tyrosine residues. Although the R2B family of RPTPs are characterized as having two tyrosine phosphatase domains in their intracellular domain, usually only one is catalytically active. A point mutation study suggests that only the first phosphatase domain of PCP-2 is catalytically active and able to dephosphorylate β-catenin. A r |
https://en.wikipedia.org/wiki/ARPC2 | Actin-related protein 2/3 complex subunit 2 is a protein that in humans is encoded by the ARPC2 gene.
Function
This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p34 subunit, has yet to be determined. Two alternatively spliced variants have been characterized to date. Additional alternatively spliced variants have been described but their full length nature has not been determined.
Interactions
ARPC2 has been shown to interact with Cortactin.
References
External links
Further reading
External links |
https://en.wikipedia.org/wiki/KIF20A | Kinesin-like protein KIF20A is a protein that in humans is encoded by the KIF20A gene.
Interactions
KIF20A has been shown to interact with RAB6A.
References
Further reading
External links |
https://en.wikipedia.org/wiki/ABI2 | Abl interactor 2 also known as Abelson interactor 2 (Abi-2) is a protein that in humans is encoded by the ABI2 gene.
Interactions
ABI2 has been shown to interact with ABL1, ADAM19, and TRIM32.
References
Further reading
External links |
https://en.wikipedia.org/wiki/ADCY5 | Adenylyl cyclase type 5 is an enzyme that in humans is encoded by the ADCY5 gene.
Interactions
ADCY5 has been shown to interact with RGS2.
Clinical significance
Mutations in ADCY5 are known to cause the following conditions:
Dyskinesia with orofacial involvement, autosomal recessive (DSKOR);
Neurodevelopmental disorder with hyperkinetic movements and dyskinesia (NEDHYD).
References
External links
Further reading
EC 4.6.1 |
https://en.wikipedia.org/wiki/ADH4 | Alcohol dehydrogenase 4 is an enzyme that in humans is encoded by the ADH4 gene.
This gene encodes class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole. This gene is localized to chromosome 4 in the cluster of alcohol dehydrogenase genes.
There is evidence that ancestors of modern humans developed the ADH4 producing gene some 10 million years ago. This probably helped them to take advantage of rotting fruit as they shifted to a terrestrial lifestyle.
References
Further reading
External links |
https://en.wikipedia.org/wiki/CENPC1 | Centromere protein C 1 is a protein that in humans is encoded by the CENPC1 gene.
Centromere protein C 1 is a centromere autoantigen and a component of the inner kinetochore plate. The protein is required for maintaining proper kinetochore size and a timely transition to anaphase. A putative pseudogene exists on chromosome 12.
References
External links
Further reading |
https://en.wikipedia.org/wiki/Collagen%2C%20type%20IX%2C%20alpha%203 | Collagen alpha-3(IX) chain is a protein that in humans is encoded by the COL9A3 gene.
Function
This gene encodes one of the three alpha chains of type IX collagen, the major collagen component of hyaline cartilage. Type IX collagen, a heterotrimeric molecule, is usually found in tissues containing type II collagen, a fibrillar collagen. Mutations in this gene are associated with multiple epiphyseal dysplasia.
References
External links
GeneReviews/NCBI/NIH/UW entry on Multiple Epiphyseal Dysplasia, Dominant
Further reading
Collagens |
https://en.wikipedia.org/wiki/Collagen%2C%20type%20XII%2C%20alpha%201 | Collagen alpha-1(XII) chain is a protein that in humans is encoded by the COL12A1 gene.
This gene encodes the alpha chain of type XII collagen, a member of the FACIT (fibril-associated collagens with interrupted triple helices) collagen family. Type XII collagen is a homotrimer found in association with type I collagen, an association that is thought to modify the interactions between collagen I fibrils and the surrounding matrix.
Alternatively spliced transcript variants encoding different isoforms have been identified.
Clinical significance
Bethlem myopathy 2 (also known as Ehlers-Danlos syndrome myopathic type) is associated with mutations in the COL12A1 gene
Ullrich congenital muscular dystrophy 2 is associated with mutations in the COL12A1 gene
References
Further reading
Collagens |
https://en.wikipedia.org/wiki/RBM14 | RNA-binding protein 14 is a protein that in humans is encoded by the RBM14 gene.
Interactions
RBM14 has been shown to interact with TARBP2.
Model organisms
Model organisms have been used in the study of RBM14 function. A conditional knockout mouse line called Rbm14tm1a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed: - In-depth immunological phenotyping
References
Further reading |
https://en.wikipedia.org/wiki/MAD2L2 | Mitotic spindle assembly checkpoint protein MAD2B is a protein that in humans is encoded by the MAD2L2 gene.
Function
MAD2L2 is a component of the mitotic spindle assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. MAD2L2 is a homolog of MAD2L1.
Interactions
MAD2L2 has been shown to interact with:
ADAM9,
MAD2L1,
REV1, and
REV3L.
References
Further reading |
https://en.wikipedia.org/wiki/UBE2E3 | Ubiquitin-conjugating enzyme E2 E3 is a protein that in humans is encoded by the UBE2E3 gene.
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. The encoded protein shares 100% sequence identity with the mouse and rat counterparts, which indicates that this enzyme is highly conserved in eukaryotes. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.
References
Further reading |
https://en.wikipedia.org/wiki/HOXB13 | Homeobox protein Hox-B13 is a protein that in humans is encoded by the HOXB13 gene.
Function
This gene encodes a transcription factor that belongs to the homeobox gene family. Genes of this family are highly conserved among vertebrates and essential for vertebrate embryonic development. This gene has been implicated in fetal skin development and cutaneous regeneration. In mice, a similar gene was shown to exhibit temporal and spatial colinearity in the main body axis of the embryo, but was not expressed in the secondary axes, which suggests functions in body patterning along the axis. This gene and other HOXB genes form a gene cluster on chromosome 17 in the 17q21-22 region.
Men who inherit a rare (<0.1% in a selected group of patients without clinical signs of prostate cancer) genetic variant in HOXB13 (G84E or rs138213197) have a 10-20-fold increased risk of prostate cancer.
See also
Homeobox
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/CREB3 | Cyclic AMP-responsive element-binding protein 3 is a protein that in humans is encoded by the CREB3 gene.
This gene encodes a transcription factor that is a member of the leucine zipper family of DNA binding proteins. This protein binds to the cAMP-responsive element, an octameric palindrome. The protein interacts with host cell factor C1, which also associates with the herpes simplex virus (HSV) protein VP16 that induces transcription of HSV immediate-early genes. This protein and VP16 both bind to the same site on host cell factor C1. It is thought that the interaction between this protein and host cell factor C1 plays a role in the establishment of latency during HSV infection. An additional transcript variant has been identified, but its biological validity has not been determined.
Interactions
CREB3 has been shown to interact with Host cell factor C1.
See also
CREB
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/ENOX2 | ENOX2 is a gene located on the long arm of the X chromosome in humans. The gene encodes the protein Ecto-NOX disulfide-thiol exchanger 2, a member of the NOX family of NADPH oxidases.
Ecto-NOX disulfide-thiol exchanger 2 is a growth-related cell surface protein. It was identified because it reacts with the monoclonal antibody K1 in cells, such as the ovarian carcinoma line OVCAR-3, also expressing the CAKI surface glycoprotein. The encoded protein has two enzymatic activities: catalysis of hydroquinone or NADH oxidation, and protein disulfide interchange. The two activities alternate with a period length of about 24 minutes. The encoded protein also displays prion-like properties. Two transcript variants encoding different isoforms have been found for this gene.
Gene Location
The human ENOX2 gene is located on the long (q) arm of the X chromosome in humans, at region 2 band 6 sub band 1, from base pair 130,622,330 to 130,903,317 (build GRCh38.p7) (map). The gene is conserved in chimpanzee, Rhesus monkey, dog, mouse, rat, chicken, and zebrafish.
Function
ENOX2 and related NOX proteins exhibit two distinct oscillating functions: the oxidation of NADH to NAD+ and a protein disulfide isomerase-like activity, unprecedented in the biochemical literature. Regarding NADH oxidation, the protein has a specific activity of 10-20μmol/min/mg of protein with a turnover number of 200-500. The oscillations are independent of temperature, with a period of 24 minutes, completing 60 cycles |
https://en.wikipedia.org/wiki/SPTLC1 | Serine palmitoyltransferase, long chain base subunit 1, also known as SPTLC1, is a protein which in humans is encoded by the SPTLC1 gene.
Serine palmitoyltransferase, which consists of two different subunits, is the initial enzyme in sphingolipid biosynthesis. It converts L-serine and palmitoyl CoA to 3-oxosphinganine with pyridoxal 5'-phosphate as a cofactor. The product of this gene is the long chain base subunit 1 of serine palmitoyltransferase. Mutations in this gene were identified in patients with hereditary sensory neuropathy type 1, macular disease, and juvenile amyotrophic lateral sclerosis. Alternatively spliced variants encoding different isoforms have been identified.
References
Further reading
External links
GeneReviews/NIH/NCBI/UW entry on Hereditary Sensory Neuropathy Type I |
https://en.wikipedia.org/wiki/ARFGEF2 | Brefeldin A-inhibited guanine nucleotide-exchange protein 2 is a protein that in humans is encoded by the ARFGEF2 gene.
Function
ADP-ribosylation factors (ARFs) play an important role in intracellular vesicular trafficking. The protein encoded by this gene is involved in the activation of ARFs by accelerating replacement of bound GDP with GTP and is involved in Golgi transport. It contains a Sec7 domain, which may be responsible for its guanine-nucleotide exchange activity and also brefeldin A inhibition.
Interactions
ARFGEF2 has been shown to interact with ARFGEF1, PRKAR1A and PRKAR2A.
References
External links
Further reading |
https://en.wikipedia.org/wiki/SIVA1 | Apoptosis regulatory protein Siva is a protein that in humans is encoded by the SIVA1 gene.
This gene encodes a protein with an important role in the apoptotic (programmed cell death) pathway induced by the CD27 antigen, a member of the tumor necrosis factor receptor (TFNR) superfamily. The CD27 antigen cytoplasmic tail binds to the N-terminus of this protein. Two alternatively spliced transcript variants encoding distinct proteins have been described.
Interactions
SIVA1 has been shown to interact with CD27.
Siva (protein)
Siva protein is a zinc-containing intracellular ligand of the CD4 receptor that promotes HIV-1 envelope-induced apoptosis in T-lymphoid cells. Recent research has demonstrated that Siva is a direct transcriptional target for the tumor-suppressors p53 and E2F1.
See also
Siva (protein)
References
Further reading |
https://en.wikipedia.org/wiki/DRAP1 | Dr1-associated corepressor is a protein that in humans is encoded by the DRAP1 gene.
Transcriptional repression is a general mechanism for regulating transcriptional initiation in organisms ranging from yeast to humans. Accurate initiation of transcription from eukaryotic protein-encoding genes requires the assembly of a large multiprotein complex consisting of RNA polymerase II and general transcription factors such as TFIIA, TFIIB, and TFIID. DR1 is a repressor that interacts with the TATA-binding protein (TBP) of TFIID and prevents the formation of an active transcription complex by precluding the entry of TFIIA and/or TFIIB into the preinitiation complex. The protein encoded by this gene is a corepressor of transcription that interacts with DR1 to enhance DR1-mediated repression. The interaction between this corepressor and DR1 is required for corepressor function and appears to stabilize the TBP-DR1-DNA complex.
Interactions
DRAP1 has been shown to interact with FOXH1 and DR1.
References
Further reading |
https://en.wikipedia.org/wiki/YKT6 | Synaptobrevin homolog YKT6 is a protein that in humans is encoded by the YKT6 gene.
Function
This gene product is one of the SNARE recognition molecules implicated in vesicular transport between secretory compartments. It is a membrane associated, isoprenylated protein that functions at the endoplasmic reticulum-Golgi transport step. This protein is highly conserved from yeast to human and can functionally complement the loss of the yeast homolog in the yeast secretory pathway.
Interactions
YKT6 has been shown to interact with BET1L.
References
Further reading |
https://en.wikipedia.org/wiki/CD226 | CD226 (Cluster of Differentiation 226), PTA1 (outdated term, 'platelet and T cell activation antigen 1') or DNAM-1 (DNAX Accessory Molecule-1) is a ~65 kDa immunoglobulin-like transmembrane glycoprotein expressed on the surface of natural killer cells, NK T cell, B cells, dendritic cells, hematopoietic precursor cells, platelets, monocytes and T cells.
DNAM-1 gene CD226 is conserved between human and mice. In humans the CD226 gene is located on chromosome 18q22.3. In mice the CD226 gene is located on chromosome 18E4.
Structure
DNAM-1 is composed of three domains: an extracellular domain of 230 amino acids with two immunoglobin-like V-set domains and eight N-glycosylation sites, a transmembrane domain of 28 amino acids and a cytosolic domain of 60 amino acids containing four putative tyrosine residues and one serine residue for phosphorylation.
Signaling
Upon engagement to its ligand, DNAM-1 is phosphorylated by protein kinase C. Then adhesive molecule LFA-1 crosslinks with DNAM-1 that results in recruitment of DNAM-1 to lipid rafts and promotes association with actin cytoskeleton. Cross-linking with LFA-1 also induce phosphorylation on Tyr128 and Tyr113 by Fyn Src kinase.
DNAM-1 and CD244 together promotes phosphorylation of SH2 domain of SLP-76. This leads to activation of phospholipase Cγ2, Ca2+ influx, cytoskeletal reorganization, degranulation, and secretion.
Function
DNAM-1 mediates cellular adhesion to other cells bearing its ligands, nectin molecule CD112 a |
https://en.wikipedia.org/wiki/CCT8 | T-complex protein 1 subunit theta is a protein that in humans is encoded by the CCT8 gene. The CCT8 protein is a component of the TRiC complex.
See also
TCP1, T-complex protein 1 subunit alpha
Chaperonin
References
External links
Further reading |
https://en.wikipedia.org/wiki/NEK6 | Serine/threonine-protein kinase Nek6 is an enzyme that in humans is encoded by the NEK6 gene.
Function
The Aspergillus nidulans 'never in mitosis A' (NIMA) gene encodes a serine/threonine kinase that controls initiation of mitosis. NIMA-related kinases (NEKs) are a group of protein kinases that are homologous to NIMA. Evidence suggests that NEKs perform functions similar to those of NIMA.
It is a protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence.
Interactions
NEK6 has been shown to interact with NEK9.
References
Further reading
Human proteins |
https://en.wikipedia.org/wiki/WASF3 | Wiskott–Aldrich syndrome protein family member 3 is a protein that in humans is encoded by the WASF3 gene.
This gene encodes a member of the Wiskott–Aldrich syndrome protein family. The gene product is a protein that forms a multiprotein complex that links receptor kinases and actin. Binding to actin occurs through a C-terminal verprolin homology domain in all family members. The multiprotein complex serves to transduce signals that involve changes in cell shape, motility or function.
See also
WASp (encoded by WAS gene)
WASF1
WASF2
References
Further reading |
https://en.wikipedia.org/wiki/TMED10 | Transmembrane emp24 domain-containing protein 10 is a protein that in humans is encoded by the TMED10 gene.
This gene is a member of the EMP24/GP25L/p24 family and encodes a protein with a GOLD domain. This type I membrane protein is localized to the plasma membrane and golgi cisternae and is involved in vesicular protein trafficking. The protein is also a member of a heteromeric secretase complex and regulates the complex's gamma-secretase activity without affecting its epsilon-secretase activity. Mutations in this gene have been associated with early-onset familial Alzheimer's disease. This gene has a pseudogene on chromosome 8.
References
Further reading |
https://en.wikipedia.org/wiki/STMN2 | Stathmin-2 is a protein that in humans is encoded by the STMN2 gene.
Function
Superior cervical ganglion-10 is a neuronal growth-associated protein which shares significant amino acid sequence similarity with the phosphoprotein stathmin (MIM 151442).[supplied by OMIM]
Interactions
STMN2 has been shown to interact with RGS6.
References
Further reading |
https://en.wikipedia.org/wiki/PNKP | Bifunctional polynucleotide phosphatase/kinase is an enzyme that in humans is encoded by the PNKP gene. A detailed structural study of the crystallized mouse protein examined both the 5´-polynucleotide kinase and 3’-polynucleotide phosphatase activities. Additional features of the peptide sequence include a forkhead association (FHA) domain, ATP binding site and nuclear and mitochondrial localization sequences.
Interactions
PNKP has been shown to interact with DNA polymerase beta and XRCC1.
Role in neurologic disease
The human gene encoding PNKP was observed to be mutated in patients with microcephaly, seizures and defects in DNA repair. A type of recessive ataxia is also associated with PNKP mutations. There are also newly characterized pathological variants of PNKP. Model organisms such as mice and Drosophila have been used to generate further insights.
References
Further reading |
https://en.wikipedia.org/wiki/SYNPO | Synaptopodin is a protein that in humans is encoded by the SYNPO gene.
Function
Synaptopodin is an actin-associated protein that may play a role in actin-based cell shape and motility. The name synaptopodin derives from the protein's associations with postsynaptic densities and dendritic spines and with renal podocytes (Mundel et al., 1997).[supplied by OMIM]
Interactions
SYNPO has been shown to interact with MAGI1.
References
Further reading |
https://en.wikipedia.org/wiki/Crystallin%2C%20beta%20A1 | Beta-crystallin A3 is a protein that in humans is encoded by the CRYBA1 gene.
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'.
References
Further read |
https://en.wikipedia.org/wiki/CRYGS | Gamma-crystallin S is a protein that in humans is encoded by the CRYGS gene.
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins.
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is monomeric and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant gamma-crystallin in adult eye lens tissue.
Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
References
External links
Further reading |
https://en.wikipedia.org/wiki/CYP3A | Cytochrome P450, family 3, subfamily A, also known as CYP3A, is a human gene locus. A homologous locus is found in mice.
The CYP3A locus includes all the known members of the 3A subfamily of the cytochrome P450 superfamily of genes. These genes encode monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. The CYP3A cluster consists of four genes:
CYP3A4,
CYP3A5,
CYP3A7, and
CYP3A43.
The region also contains four pseudogenes:
,
,
, and
.
as well as several extra exons which may or may not be included in transcripts produced from this region. Previously another CYP3A member, CYP3A3, was thought to exist; however, it is now thought that this sequence represents a transcript variant of CYP3A4.
References
Further reading
3
EC 1.14.14 |
https://en.wikipedia.org/wiki/DGKA | Diacylglycerol kinase alpha is an enzyme that in humans is encoded by the DGKA gene.
The protein encoded by this gene belongs to the eukaryotic diacylglycerol kinase family. It acts as a modulator that competes with protein kinase C for the second messenger diacylglycerol in intracellular signaling pathways. It also plays an important role in the resynthesis of phosphatidylinositols and phosphorylating diacylglycerol to phosphatidic acid. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified.
References
Further reading
*
External links
DAG-kinase catalytic (DAGKc) domain in PROSITE
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/DDX6 | Probable ATP-dependent RNA helicase DDX6 is an enzyme that in humans is encoded by the DDX6 gene.
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein. It may contribute to the cell proliferation and carcinogenesis.
References
Further reading |
https://en.wikipedia.org/wiki/DR1%20%28gene%29 | Protein Dr1 is a protein that in humans is encoded by the DR1 gene.
Function
This gene encodes a TBP- (TATA box-binding protein) associated phosphoprotein that represses both basal and activated levels of transcription. The encoded protein is phosphorylated in vivo and this phosphorylation affects its interaction with TBP. This protein contains a histone fold motif at the amino terminus, a TBP-binding domain, and a glutamine- and alanine-rich region. The binding of DR1 repressor complexes to TBP-promoter complexes may establish a mechanism in which an altered DNA conformation, together with the formation of higher order complexes, inhibits the assembly of the preinitiation complex and controls the rate of RNA polymerase II transcription.
Interactions
DR1 (gene) has been shown to interact with DRAP1.
References
Further reading |
https://en.wikipedia.org/wiki/DVL2 | Segment polarity protein dishevelled homolog DVL-2 is a protein that in humans is encoded by the DVL2 gene.
This gene encodes a member of the dishevelled (dsh) protein family. The vertebrate dsh proteins have approximately 40% amino acid sequence similarity with Drosophila dsh. This gene encodes a 90-kD protein that undergoes posttranslational phosphorylation to form a 95-kD cytoplasmic protein, which may play a role in the signal transduction pathway mediated by multiple Wnt proteins. The mechanisms of dishevelled function in Wnt signaling are likely to be conserved among metazoans.
Interactions
DVL2 has been shown to interact with Zinc finger protein 165, DAB2 and Arrestin beta 1.
See also
Dishevelled
References
Further reading |
https://en.wikipedia.org/wiki/EIF5 | Eukaryotic translation initiation factor 5 is a protein that in humans is encoded by the EIF5 gene.
EIF5 is a GTPase-activating protein.
References
External links
Cap-dependent translation initiation from Nature Reviews Microbiology. A good image and overview of the function of initiation factors
PDBe-KB provides an overview of all the structure information available in the PDB for Human Eukaryotic translation initiation factor 5 (EIF5)
Further reading |
https://en.wikipedia.org/wiki/SERPINB1 | Leukocyte elastase inhibitor (LEI) also known as serpin B1 is a protein that in humans is encoded by the SERPINB1 gene. It is a member of the clade B serpins or ov-serpins (ovalbumin related serpins) founded by ovalbumin.
MNEI (monocyte/neutrophil elastase inhibitor) is the mouse orthologue of human SerpinB1.
Function
SerpinB1 is a cytoplasmic serine protease inhibitor of polymorphonuclear neutrophils. Among other serine proteases, it specifically inhibits neutrophil elastase, PR3 and cathepsin G, all found in neutrophil granules, by a suicide inhibition mechanism. SerpinB1 was found to reduce tissue damage caused by the mentioned proteases during inflammation and has a role in neutrophil homeostasis in mice. In various infection models (e.g. pneumonia) correlation of SerpinB1 absence and lack of microbial clearance have been shown. Different knockout strains serve as model to investigate the role of SerpinB1 in vivo.
See also
Serpin
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: I04.006
Serine protease inhibitors |
https://en.wikipedia.org/wiki/FABP7 | Fatty acid binding protein 7, brain (FABP7; also brain lipid binding protein, BLBP), is a human gene.
Function
The protein encoded by this gene is a brain fatty acid binding protein. Fatty acid binding proteins (FABPs) are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs are thought to play roles in fatty acid uptake, transport, and metabolism.
FABP7 is expressed, during development, in radial glia by the activation of Notch receptors. Reelin was shown to induce FABP7 expression in neural progenitor cells via Notch-1 activation.
According to one study, FABP7 binds DHA with the highest affinity among all of the FABPs.
Role in pathology
FABP7 maps onto human chromosome 6q22.31, a schizophrenia linkage region corroborated by a meta-analysis.
As of 2008, two studies have been conducted into FABP7 as a possible risk gene for schizophrenia, with one, that tested for only one SNP, showing negative and another, with seven SNPs, a positive result. The effect of the gene in the latter study was stronger in males. This study also linked FABP7 variation to weak prepulse inhibition in mice; deficit in PPI is an endophenotypic trait observed in schizophrenia patients and their relatives.
References
Further reading
External links
Schizophrenia, Startled Response & Fabp7: Future Dietary Changes for At-Risk Mothers? Schizophrenia Daily News Blog, 2007-11-07
- a synopsis for the general audience.
Biol |
https://en.wikipedia.org/wiki/ACSL1 | Long-chain-fatty-acid—CoA ligase 1 is an enzyme that in humans is encoded by the ACSL1 gene.
Structure
Gene
The ACSL1 gene is located on the 4th chromosome, with its specific location being 4q35.1. The gene contains 28 exons.
The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation.
In melanocytic cells ACSL1 gene expression may be regulated by MITF.
Function
The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. Several transcript variants encoding different isoforms have been found for this gene. This specific protein is most commonly found in mitochondria and peroxisomes.
Clinical significance
ACSL1 is known to be involved in fatty-acid metabolism critical for heart function and nonspecific mental retardation. Since the ACSL4 gene is highly expressed in brain, where it encodes a brain specific isoform, an ASCL1 mutation may be an effic |
https://en.wikipedia.org/wiki/FLII | Protein flightless-1 homolog is a protein that in humans is encoded by the FLII gene.
This gene encodes a protein with a gelsolin-like actin binding domain and an N-terminal leucine-rich repeat-protein protein interaction domain. The protein is similar to a Drosophila protein involved in early embryogenesis and the structural organization of indirect flight muscle. The gene is located within the Smith-Magenis syndrome region on chromosome 17.
Interactions
FLII has been shown to interact with LRRFIP1 and TRAF interacting protein.
References
Further reading |
https://en.wikipedia.org/wiki/MLANA | Protein melan-A also known as melanoma antigen recognized by T cells 1 or MART-1 is a protein that in humans is encoded by the MLANA or "MALENA" gene. A fragment of the protein, usually consisting of the nine amino acids 27 to 35, is bound by MHC class I complexes which present it to T cells of the immune system. These complexes can be found on the surface of melanoma cells. Decameric peptides (26-35) are being investigated as cancer vaccines.
Discovery and nomenclature
The names MART-1 and melan-A were coined by two groups of researchers who independently sequenced the gene for this antigen in 1994. Both names are currently in common use. Kawakami et al. at the National Cancer Institute coined the term MART-1, which stands for "melanoma antigen recognized by T-cells." Coulie et al. of Belgium called the gene melan-A, presumably an abbreviation for "melanocyte antigen."
Clinical significance
MART-1/melan-A is a protein antigen that is found on the surface of melanocytes. Antibodies against the antigen are used in the medical specialty of anatomic pathology in order to recognize cells of melanocytic differentiation, useful for the diagnosis of a melanoma. The same name is also used to refer to the gene which codes for the antigen.
The MART-1/melan-A antigen is specific for the melanocyte lineage, found in normal skin, the retina, and melanocytes, but not in other normal tissues. It is thus useful as a marker for melanocytic tumors (melanomas) with the caveat that |
https://en.wikipedia.org/wiki/GABPB2 | GA-binding protein subunit beta-1 is a protein that in humans is encoded by the GABPB1 gene.
This gene encodes the GA-binding protein transcription factor, beta subunit. This protein forms a tetrameric complex with the alpha subunit, and stimulates transcription of target genes. The encoded protein may be involved in activation of cytochrome oxidase expression and nuclear control of mitochondrial function. The crystal structure of a similar protein in mouse has been resolved as a ternary protein complex. Multiple transcript variants encoding distinct isoforms have been identified for this gene.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/COPG | Coatomer subunit gamma is a protein that in humans is encoded by the COPG gene. It is one of seven proteins in the COPI coatomer complex that coats vesicles as they bud from the Golgi complex.
Interactions
COPG has been shown to interact with Dopamine receptor D1, COPZ1 and COPB1.
References
External links
Further reading |
https://en.wikipedia.org/wiki/MAST2 | Microtubule-associated serine/threonine-protein kinase 2 is an enzyme that in humans is encoded by the MAST2 gene. The protein encoded by this gene controls TRAF6 and NF-kappaB activity.
Interactions
MAST2 has been shown to interact with PCLKC.
Model organisms
Model organisms have been used in the study of MAST2 function. A conditional knockout mouse line called Mast2tm1a(KOMP)Wtsi has been generated. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed: - In-depth immunological phenotyping
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/SYNE2 | Nesprin-2 is a protein that in humans is encoded by the SYNE2 gene. The human SYNE2 gene consists of 116 exons and encodes nesprin-2, a member of the nuclear envelope (NE) spectrin-repeat (nesprin) family. Nesprins are modular proteins with a central extended spectrin-repeat (SR) rod domain and a C-terminal Klarsicht/ANC-1/Syne homology (KASH) transmembrane domain, which acts as a NE-targeting motif. Nesprin-2 (Nesp2) binds to cytoplasmic F-actin, tethering the nucleus to the cytoskeleton and maintaining the structural integrity of the nucleus.
The human SYNE2 gene encodes a protein of 6,885 amino acids (isoform 1, Nesp2 giant); alternative mRNA splicing produces transcripts encoding a larger isoform and numerous smaller isoforms, some of which are specific to various tissues; alternative start and termination sites within the mRNA also allow translation of smaller isoforms, many possessing unique N- or C-terminal sequences encoded by retained introns. Two mechanisms create splice variants of nesprin-2 with the KASH domain deleted (deltaKASH). In deltaKASH1 variants, deletion of cassette exons 111-112 results in a frame shift that disrupts the KASH domain but retains the 3' untranslated region (UTR) in exon 116 utilized for isoforms containing the KASH domain. This mechanism, which also occurs in SYNE1 mRNA encoding nesprin-1 (enaptin), generates deltaKASH1 isoforms terminating with a distinct 11-amino acid tail (GIAGHSATPPA replacing YPMLRYTNGPPPT in isoforms with KASH). Ut |
https://en.wikipedia.org/wiki/CLASP1 | Cytoplasmic linker associated protein 1, also known as CLASP1, is a protein which in humans is encoded by the CLASP1 gene.
Function
CLASP1 belongs to a family of microtubule-associated proteins involved in attachment of microtubules to the cell cortex in animals and plants. CLASPs, such as CLASP1, interact with CLIPs (e.g., CLIP1). In animal cells, CLASP1 is involved in the regulation of microtubule dynamics at the kinetochore and throughout the spindle. CLASP1 controls the interactions of astral microtubules with the cell cortex in mitosis, which is important for the proper positioning and orientation of the spindle.
References
External links
Further reading |
https://en.wikipedia.org/wiki/PIP5K1C | Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma is an enzyme that in humans is encoded by the PIP5K1C gene.
This gene encodes a member of the type I phosphatidylinositol-4-phosphate 5-kinase family of enzymes. A similar protein in mice is found in synapses and focal adhesion plaques, and binds the FERM domain of talin through its C-terminus.
Model organisms
Model organisms have been used in the study of PIP5K1C function. A conditional knockout mouse line, called Pip5k1ctm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty three tests were carried out on mutant mice and two significant abnormalities were observed. Fewer than expected homozygous mutant embryos were identified during gestation, and none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice and no further phenotypes were observed.
References
Further reading
Genes mutated in mice |
https://en.wikipedia.org/wiki/BRD4 | Bromodomain-containing protein 4 is a protein that in humans is encoded by the BRD4 gene.
BRD4 is a member of the BET (bromodomain and extra terminal domain) family, which also includes BRD2, BRD3, and BRDT. BRD4, similar to other BET family members, contains two bromodomains that recognize acetylated lysine residues. BRD4 also has an extended C-terminal domain with little sequence homology to other BET family members.
Structure
The two bromodomains in BRD4, termed BD1 and BD2, consist of 4 alpha-helices linked by 2 loops. The ET domain structure is made up of 3 alpha-helices and a loop. The C-terminal domain of BRD4 has been implicated in promoting gene transcription through interaction with the transcription elongation factor P-TEFb and RNA polymerase II.
Function
The protein encoded by this gene is homologous to the murine protein MCAP, which associates with chromosomes during mitosis, and to the human BRD2 (RING3) protein, a serine/threonine kinase. Each of these proteins contains two bromodomains, a conserved sequence motif which may be involved in chromatin targeting. This gene has been implicated as the chromosome 19 target of translocation t(15;19)(q13;p13.1), which defines the NUT midline carcinoma. Two alternatively spliced transcript variants have been described.
Role in cancer
Most cases of NUT midline carcinoma involve translocation of the BRD4 gene with NUT genes. BRD4 is often required for expression of Myc and other "tumor driving" oncogenes in hema |
https://en.wikipedia.org/wiki/SNAPAP | SNARE-associated protein Snapin is a protein that in humans is encoded by the SNAPIN gene.
Function
SNAPAP is a component of the SNARE complex of proteins that is required for synaptic vesicle docking and fusion. SNAPAP is also a component of the ubiquitously expressed BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.
Snapin has been established to be a promoter of vesicle docking, as it plays a role in binding to SNAP-25, which together stabilize and favor SNARE complex assembly and vesicle docking. Specifically, the degree to which snapin is necessary for proper synaptic release varies across species. The functions of snapin have been reported to be independent of synaptotagmin, and works through the SNAP-25 pathway to stabilize, prime, and dock vesicles.
Interactions
SNAPAP has been shown to interact with:
BLOC1S1,
BLOC1S2,
Dysbindin,
PLDN,
RGS7,
SNAP-25,
SNAP23, and
TRPV1.
References
Further reading |
https://en.wikipedia.org/wiki/TRIM29 | Tripartite motif-containing protein 29 is a protein that in humans is encoded by the TRIM29 gene.
Function
The protein encoded by this gene belongs to the TRIM protein family. It has multiple zinc finger motifs and a leucine zipper motif. It has been proposed to form homo- or heterodimers which are involved in nucleic acid binding. Thus, it may act as a transcriptional regulatory factor involved in carcinogenesis and/or differentiation. It may also function in the suppression of radiosensitivity since it is associated with ataxia–telangiectasia phenotype.
Interactions
TRIM29 has been shown to interact with TRIM23 and GCC1.
References
Further reading |
https://en.wikipedia.org/wiki/STX12 | Syntaxin-12 is a protein that in humans is encoded by the STX12 gene.
Interactions
STX12 has been shown to interact with PLDN.
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Syntaxin-12 |
https://en.wikipedia.org/wiki/MTPN | Myotrophin is a protein that in humans is encoded by the MTPN gene.
Interactions
MTPN has been shown to interact with RELA and REL.
References
Further reading |
https://en.wikipedia.org/wiki/Alpha-taxilin | Alpha-taxilin also known as interleukin-14 (IL-14) or high molecular weight B-cell growth factor (HMW-BCGF) is a protein that in humans is encoded by the TXLNA gene.
Interleukin-14 is a cytokine that controls the growth and proliferation of both normal and cancerous B cells. This molecule was also recently designated taxilin. IL-14 induces B-cell proliferation, inhibits antibody secretion, and expands selected B-cell subgroups. This interleukin is produced mainly by T cells and certain malignant B cells.
Gene
In murine models, two distinct transcripts are produced from opposite strands of the il14 gene that are called IL-14α and IL-14β. The il14 locus is near the gene for LCK on chromosome 1 in humans.
References
External links
Further reading
Interleukins |
https://en.wikipedia.org/wiki/GFI1 | Zinc finger protein Gfi-1 is a transcriptional repressor that in humans is encoded by the GFI1 gene. It is important normal hematopoiesis.
Interactions
GFI1 has been shown to interact with PIAS3 and RUNX1T1.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/GOLGA3 | Golgin subfamily A member 3 is a protein that in humans is encoded by the GOLGA3 gene.
The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Interactions between the Golgi and microtubules are thought to be important for the reorganization of the Golgi after it fragments during mitosis.
This gene encodes a member of the golgin family of proteins which are localized to the Golgi. Its encoded protein has been postulated to play a role in nuclear transport and Golgi apparatus localization. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of these variants has not been determined.
References
Further reading |
https://en.wikipedia.org/wiki/GOLGA4 | Golgin subfamily A member 4 is a protein that in humans is encoded by the GOLGA4 gene.
The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Interactions between the Golgi and microtubules are thought to be important for the reorganization of the Golgi after it fragments during mitosis. The golgins are a family of proteins, of which the protein encoded by this gene is a member, that are localized to the Golgi. This protein has been postulated to play a role in Rab6-regulated membrane-tethering events in the Golgi apparatus. Alternative splice variants have been described but their full-length nature has not been determined.
Interactions
GOLGA4 has been shown to interact with ARL1.
References
Further reading |
https://en.wikipedia.org/wiki/GP5%20%28gene%29 | Glycoprotein V (platelet) (GP5) also known as CD42d (Cluster of Differentiation 42d), is a human gene.
Human platelet glycoprotein V (GP5) is a part of the Ib-V-IX system of surface glycoproteins that constitute the receptor for von Willebrand factor (VWF; MIM 193400) and mediate the adhesion of platelets to injured vascular surfaces in the arterial circulation, a critical initiating event in hemostasis. The main portion of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain (GP1BA; MIM 606672) and a beta chain (GP1BB; MIM 138720), that are linked by disulfide bonds. The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX (GP9; MIM 173515) and GP5. Mutations in GP1BA, GP1BB, and GP9 have been shown to cause Bernard-Soulier syndrome (MIM 231200), a bleeding disorder.[supplied by OMIM]
See also
Cluster of differentiation
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/GSTZ1 | Glutathione S-transferase Zeta 1 (also known as maleylacetoacetate isomerase) is an enzyme that in humans is encoded by the GSTZ1 gene on chromosome 14.
This gene is a member of the glutathione S-transferase (GSTs) super-family, which encodes multifunctional enzymes important in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. This enzyme also plays a significant role in the catabolism of phenylalanine and tyrosine. Thus, defects in this enzyme may lead to severe metabolic disorders, including alkaptonuria, phenylketonuria and tyrosinaemia, and new discoveries may allow the enzyme to protect against certain diseases related to oxidative stress.
Structure
Glutathione S-transferase Zeta 1 (GSTZ1) has a predominantly hydrophobic dimer, just like many other GST members. It is composed of 24.2 kDa subunits and it consists of an N-terminal thioredoxin-like domain and a C-terminal all alpha-helical domain. Both of these domains are intertwined by a linker region between amino acids 85 and 91. The active site of this enzyme is much smaller and more polar than that of other family members of GST, which allows for GSTZ1 to be more selective in terms of substrates. Also, the C-terminus is truncated and the GSTZ1 enzyme lacks the normal V-shaped dimer interface which are usually common in other GSTs. As for the GSTZ1 gene, it is located on chromosome 14q24.3, has 12 exons, and is approximatel |
https://en.wikipedia.org/wiki/GTF3C2 | General transcription factor 3C polypeptide 2 is a protein that in humans is encoded by the GTF3C2 gene.
Interactions
GTF3C2 has been shown to interact with GTF3C4 and GTF3C5.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/HNRPH3 | Heterogeneous nuclear ribonucleoprotein H3 is a protein that in humans is encoded by the HNRNPH3 gene.
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA).
These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties.
The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs. It is localized in nuclear bodies of the nucleus. This protein is involved in the splicing process and it also participates in early heat shock-induced splicing arrest by transiently leaving the hnRNP complexes. Multiple alternative transcript variants seem to be present for this gene and some appear to have intronic regions in the mRNA. Presently, only two transcript variants are fully described.
References
Further reading |
https://en.wikipedia.org/wiki/HOXA4 | Homeobox A4, also known as HOXA4, is a protein which in humans is encoded by the HOXA4 gene.
Function
In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor which may regulate gene expression, morphogenesis, and differentiation.
See also
Homeobox
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/HYAL1 | Hyaluronidase-1 is an enzyme that in humans is encoded by the HYAL1 gene.
Function
This gene encodes a lysosomal hyaluronidase. Hyaluronidases intracellularly degrade hyaluronan, one of the major glycosaminoglycans of the extracellular matrix. Hyaluronan is thought to be involved in cell proliferation, migration and differentiation. This enzyme is active at an acidic pH and is the major hyaluronidase in plasma. Mutations in this gene are associated with mucopolysaccharidosis type IX, or hyaluronidase deficiency. The gene is one of several related genes in a region of chromosome 3p21.3 associated with tumor suppression. Multiple transcript variants encoding different isoforms have been found for this gene.
Structure
HYAL1 was first purified from human plasma and urine. The enzyme is 435 amino acids long with a molecular weight of 55-60 kDa.
The crystal structure of HYAL1 was determined by Chao, Muthukumar, and Herzberg. The enzyme is composed of two closely associated domains: a N-terminal catalytic domain (Phe22-Thr352) and a smaller C-terminal domain (Ser353-Trp435). The catalytic domain adopts a distorted (β/α)8 barrel fold similar to that of bee venom hyaluronidase. Within the catalytic domain, residues such as Tyr247, Asp129, Glu131, Asn350, and Tyr202 play important roles in the cleavage of the β1→4 linkage between N-acetylglucosamine and glucuronic acid units in hyaluronan.
Mechanism
HYAL1 is responsible for the hydrolysis of intracellular hyaluronan of all |
https://en.wikipedia.org/wiki/IFI27 | Interferon alpha-inducible protein 27 is a protein that in humans is encoded by the IFI27 gene.
References
Further reading |
https://en.wikipedia.org/wiki/IGFALS | Insulin-like growth factor binding protein, acid labile subunit, also known as IGFALS, is a protein which in humans is encoded by the IGFALS gene.
Function
The protein encoded by this gene is a serum protein that binds insulin-like growth factors, increasing their half-life and their vascular localization. Production of the encoded protein, which contains twenty leucine-rich repeats, is stimulated by growth hormone. Three transcript variants encoding two different isoforms have been found for this gene.
Clinical significance
Defects in this gene are a cause of acid-labile subunit deficiency, which manifests itself in a delayed and slow puberty.
Interactions
IGFALS has been shown to interact with IGFBP3.
References
Further reading |
https://en.wikipedia.org/wiki/IGH%40 | Immunoglobulin heavy locus, also known as IGH, is a region on human chromosome 14 that contains a gene for the heavy chains of human antibodies (or immunoglobulins).
Immunoglobulins recognize foreign antigens and initiate immune responses such as phagocytosis and the complement system. Each immunoglobulin molecule consists of two identical heavy chains and two identical light chains. This region represents the germline organization of the heavy chain locus. The locus includes V (variable), D (diversity), J (joining), and C (constant) segments. During B cell development, a recombination event at the DNA level joins a single D segment with a J segment; the fused D-J exon of this partially rearranged D-J region is then joined to a V segment. The rearranged V-D-J region containing a fused V-D-J exon is then transcribed and fused at the RNA level to the IGHM constant region; this transcript encodes a mu heavy chain. Later in development B cells generate V-D-J-Cmu-Cdelta pre-messenger RNA, which is alternatively spliced to encode either a mu or a delta heavy chain. Mature B cells in the lymph nodes undergo switch recombination, so that the fused V-D-J gene segment is brought in proximity to one of the IGHG, IGHA, or IGHE gene segments and each cell expresses either the gamma, alpha, or epsilon heavy chain. Potential recombination of many different V segments with several J segments provides a wide range of antigen recognition. Additional diversity is attained by junctional diversi |
https://en.wikipedia.org/wiki/FBXO7 | F-box only protein 7 is a protein that in humans is encoded by the FBXO7 gene. Mutations in FBXO7 have been associated with Parkinson's disease.
Function
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class and it may play a role in regulation of hematopoiesis. Alternatively spliced transcript variants of this gene have been identified with the full-length natures of only some variants being determined.
Interactions
FBXO7 has been shown to interact with SKP1A, CUL1, CDK6, p27, PI31, Parkin, and PINK1.
References
Further reading |
https://en.wikipedia.org/wiki/PRKD2 | Serine/threonine-protein kinase D2 or PKD2 is an enzyme that in humans is encoded by the PRKD2 gene.
Function
The protein encoded by this gene belongs to the protein kinase D (PKD) family of serine/threonine protein kinases, a subfamily of protein kinase c. This kinase can be activated by phorbol esters as well as by gastrin via the cholecystokinin B receptor (CCKBR) in gastric cancer cells. It can bind to diacylglycerol (DAG) in the trans-Golgi network (TGN) and may regulate basolateral membrane protein exit from TGN. Alternative splicing results in multiple transcript variants encoding different isoforms.
References
Further reading
EC 2.7.11 |
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