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https://en.wikipedia.org/wiki/XRCC2 | DNA repair protein XRCC2 is a protein that in humans is encoded by the XRCC2 gene.
Function
This gene encodes a member of the RecA/Rad51-related protein family that participates in homologous recombination to maintain chromosome stability and repair DNA damage. This gene is involved in the repair of DNA double-strand breaks by homologous recombination and it functionally complements Chinese hamster irs1, a repair-deficient mutant that exhibits hypersensitivity to a number of different DNA-damaging agents.
The XRCC2 protein is one of five human paralogs of RAD51, including RAD51B (RAD51L1), RAD51C (RAD51L2), RAD51D (RAD51L3), XRCC2 and XRCC3. They each share about 25% amino acid sequence identity with RAD51 and each other.
The RAD51 paralogs are all required for efficient DNA double-strand break repair by homologous recombination and depletion of any paralog results in significant decreases in homologous recombination frequency.
XRCC2 forms a four-part complex with three related paralogs: BCDX2 (RAD51B-RAD51C-RAD51D-XRCC2) while two paralogs form a second complex CX3 (RAD51C-XRCC3). These two complexes act at two different stages of homologous recombinational DNA repair. The BCDX2 complex is responsible for RAD51 recruitment or stabilization at damage sites. The BCDX2 complex appears to act by facilitating the assembly or stability of the RAD51 nucleoprotein filament.
The CX3 complex acts downstream of RAD51 recruitment to damage sites. The CX3 complex was shown to |
https://en.wikipedia.org/wiki/PSCA%20%28gene%29 | Prostate stem cell antigen is a protein that in humans is encoded by the PSCA gene.
This gene encodes a glycosylphosphatidylinositol-anchored cell membrane glycoprotein. In addition to being highly expressed in the prostate it is also expressed in the bladder, placenta, colon, kidney, and stomach. This gene has a nonsynonymous nucleotide polymorphism at its start codon.
Clinical significance
This gene is up-regulated in a large proportion of prostate cancers and is also detected in cancers of the bladder and pancreas.
Mechanism
A study reviewing the potential role of PSCA proposed that expression of the gene is regulated through the androgen receptor complex. The proteins translated from the gene, is then glycosylated in the ER, and transported to the cell membrane where it is connected to a lipid. This results in the formation of a GPI-anchored proteins, these proteins can be often secreted by cells or play a role in cell signaling. While, the ligand activating PSCA or the downstream physiological role has not yet been determined, because of its mechanism and over expression in prostate cancer cells, PSCA can potentially serve as a biomarker for detecting cancer.
References
Further reading |
https://en.wikipedia.org/wiki/TAF15 | TATA-binding protein-associated factor 2N is a protein that in humans is encoded by the TAF15 gene.
Function
Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes a subunit of TFIID present in a subset of TFIID complexes. Translocations involving chromosome 17 and chromosome 9, where the gene for the nuclear receptor CSMF is located, result in a gene fusion product that is an RNA binding protein associated with a subset of extraskeletal myxoid chondrosarcomas. Two transcripts encoding different isoforms have been identified.
Interactions
TAF15 has been shown to interact with:
POLR2C,
POLR2E,
POLR2G,
SAFB,
TAF11,
TAF13,
TAF5,
TAF7, and
TATA binding protein
References
Further reading
External links |
https://en.wikipedia.org/wiki/SF3A2 | Splicing factor 3A subunit 2 is a protein that in humans is encoded by the SF3A2 gene.
Function
This gene encodes subunit 2 of the splicing factor 3a protein complex. The splicing factor 3a heterotrimer includes subunits 1, 2 and 3 and is necessary for the in vitro conversion of 15S U2 snRNP into an active 17S particle that performs pre-mRNA splicing. Subunit 2 interacts with subunit 1 through its amino-terminus while the single zinc finger domain of subunit 2 plays a role in its binding to the 15S U2 snRNP. Subunit 2 may also function independently of its RNA splicing function as a microtubule-binding protein.
Interactions
SF3A2 has been shown to interact with DDX46.
References
Further reading |
https://en.wikipedia.org/wiki/CHAF1B | Chromatin assembly factor 1 subunit B is a protein that in humans is encoded by the CHAF1B gene.
Function
Chromatin assembly factor I (CAF-1) is required for the assembly of histone octamers onto newly-replicated DNA. CAF-I is composed of three protein subunits, p50, p60, and p150. The protein encoded by this gene corresponds to the p60 subunit and is required for chromatin assembly after replication. The encoded protein is differentially phosphorylated in a cell cycle-dependent manner. In addition, it is normally found in the nucleus except during mitosis, when it is released into the cytoplasm. This protein is a member of the WD-repeat HIR1 family and may also be involved in DNA repair.
Interactions
CHAF1B has been shown to interact with:
ASF1A,
ASF1B, and
BAZ1B.
References
Further reading
External links |
https://en.wikipedia.org/wiki/N-alpha-acetyltransferase%2010 | N-alpha-acetyltransferase 10 (NAA10) also known as NatA catalytic subunit Naa10 and arrest-defective protein 1 homolog A (ARD1A) is an enzyme subunit that in humans is encoded NAA10 gene.
Together with its auxiliary subunit Naa15, Naa10 constitutes the NatA (Nα-acetyltransferase A) complex that specifically catalyzes the transfer of an acetyl group from acetyl-CoA to the N-terminal primary amino group of certain proteins. In higher eukaryotes, 5 other N-acetyltransferase (NAT) complexes, NatB-NatF, have been described that differ both in substrate specificity and subunit composition.
Gene and transcripts
The human NAA10 is located on chromosome Xq28 and contains 8 exons, 2 encoding three different isoforms derived from alternate splicing. Additionally, a processed NAA10 gene duplication NAA11 (ARD2) has been identified that is expressed in several human cell lines; however, later studies indicate that Naa11 is not expressed in the human cell lines HeLa and HEK293 or in cancerous tissues, and NAA11 transcripts were only detected in testicular and placental tissues. Naa11 has also been found in mouse, where it is mainly expressed in the testis. NAA11 is located on chromosome 4q21.21 in human and 5 E3 in mouse, and only contains two exons. Mice have another Naa10-like paralog, Naa12. Naa12 has NAT activity and genetically compensates for loss of Naa10, while being Naa10/Naa12 null is embryonic lethal in mic.
In mouse, NAA10 is located on chromosome X A7.3 and contains 9 exon |
https://en.wikipedia.org/wiki/AXIN2 | Axin-2, also known as axin-like protein (Axil), axis inhibition protein 2 (AXIN2), or conductin, is a protein that in humans is encoded by the AXIN2 gene.
Function
The Axin-related protein, Axin2, presumably plays an important role in the regulation of the stability of beta-catenin in the Wnt signaling pathway, like its rodent homologs, mouse conductin/rat axil. In mouse, conductin organizes a multiprotein complex of APC (adenomatous polyposis of the colon), beta-catenin, glycogen synthase kinase 3-beta, and conductin, which leads to the degradation of beta-catenin.
The AXIN proteins attract substantial interest in cancer research as AXIN1 and AXIN2 work synergistically to control pro-oncogenic β-catenin signaling. Importantly, activity in the β-catenin destruction complex can be increased by tankyrase inhibitors and are a potential therapeutic option to reduce the growth of β-catenin-dependent cancers.
Clinical significance
The deregulation of beta-catenin is an important event in the genesis of a number of malignancies. The AXIN2 gene has been mapped to 17q23-q24, a region that shows frequent loss of heterozygosity in breast cancer, neuroblastoma, and other tumors. Mutations in this gene have been associated with colorectal cancer with defective mismatch repair.
The most critical events of teeth, lip and palate formation occur almost concurrently. Hypodontia, defined as the congenital lack of one or more permanent teeth, is the most common dental abnormality found in |
https://en.wikipedia.org/wiki/HIST1H2AM | Histone H2A type 1 is a protein that in humans is encoded by the HIST1H2AM gene.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3.
References
Further reading |
https://en.wikipedia.org/wiki/AP3B1 | AP-3 complex subunit beta-1 is a protein that in humans is encoded by the AP3B1 gene.
Function
This gene encodes a protein that may play a role in organelle biogenesis associated with melanosomes, platelet dense granules, and lysosomes. The encoded protein is part of the heterotetrameric AP-3 protein complex which interacts with the scaffolding protein clathrin. Mutations in this gene are associated with Hermansky–Pudlak syndrome type 2.
Interactions
AP3B1 has been shown to interact with AP3S2.
References
External links
GeneReviews/NCBI/NIH/UW entry on Hermansky-Pudlak Syndrome
Further reading |
https://en.wikipedia.org/wiki/MADD%20%28gene%29 | MAP kinase-activating death domain protein is an enzyme that in humans is encoded by the MADD gene.
Tumor necrosis factor alpha (TNF-alpha) is a signaling molecule that interacts with one of two receptors on cells targeted for apoptosis. The apoptotic signal is transduced inside these cells by cytoplasmic adaptor proteins. The protein encoded by this gene is a death domain-containing adaptor protein that interacts with the death domain of TNF-alpha receptor 1 to activate mitogen-activated protein kinase (MAPK) and propagate the apoptotic signal. It is membrane-bound and expressed at a higher level in neoplastic cells than in normal cells. Several transcript variants encoding different isoforms have been described for this gene.
References
Further reading |
https://en.wikipedia.org/wiki/EIF3I | Eukaryotic translation initiation factor 3 subunit I (eIF3i) is a protein that in humans is encoded by the EIF3I gene.
Interactions
eIF3i has been shown to interact with TGF beta 1 and eIF3a.
See also
Eukaryotic initiation factor 3 (eIF3)
References
Further reading |
https://en.wikipedia.org/wiki/Polycomb%20protein%20EED | Polycomb protein EED is a protein that in humans is encoded by the EED gene.
Function
Polycomb protein EED is a member of the Polycomb-group (PcG) family. PcG family members form multimeric protein complexes, which are involved in maintaining the transcriptional repressive state of genes over successive cell generations. This protein interacts with enhancer of zeste 2, the cytoplasmic tail of integrin β7, immunodeficiency virus type 1 (HIV-1) MA protein, and histone deacetylase proteins. This protein mediates repression of gene activity through histone deacetylation, and may act as a specific regulator of integrin function. Two transcript variants encoding distinct isoforms have been identified for this gene.
Clinical significance
In humans, a de-novo mutation in EED has been reported in an individual displaying symptoms similar to those of Weaver syndrome.
Interactions
EED has been shown to interact with:
EZH2,
HDAC1,
Histone deacetylase 2,
ITGB7,
PPP1R8, and
TGS1.
References
External links
Further reading |
https://en.wikipedia.org/wiki/GBF1 | Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 is a protein that in humans is encoded by the GBF1 gene.
References
Further reading |
https://en.wikipedia.org/wiki/Carboxylesterase%202 | Carboxylesterase 2 is an enzyme that in humans is encoded by the CES2 gene. It is a member of the alpha/beta fold hydrolase family.
Carboxylesterase 2 is a member of a large multigene family. The enzymes encoded by these genes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. The specific function of this enzyme has not yet been determined; however, it is speculated that carboxylesterases may play a role in lipid metabolism and/or the blood–brain barrier system. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
Interactive pathway map
References
Further reading |
https://en.wikipedia.org/wiki/Far%20upstream%20element-binding%20protein%201 | Far upstream element-binding protein 1 is a protein that in humans is encoded by the FUBP1 gene.
This gene encodes a ssDNA binding protein that activates the far upstream element (FUSE) of c-myc and stimulates expression of c-myc in undifferentiated cells. Regulation of FUSE by FUBP occurs through single-strand binding of FUBP to the non-coding strand. This protein has been shown to function as an ATP-dependent DNA helicase.
Interactions
Far upstream element-binding protein 1 has been shown to interact with MAPK14 and SMN1.
Clinical Significance
FUBP1 gene deletion forms part of the 1p/19q codeletion mutation seen in oligodendroglioma, a form of primary brain tumour. CIC gene is also lost in the 1p/19q codeletion mutation.
References
Further reading |
https://en.wikipedia.org/wiki/EIF2B3 | Translation initiation factor eIF-2B subunit gamma is a protein that in humans is encoded by the EIF2B3 gene.
References
Further reading |
https://en.wikipedia.org/wiki/LY6E | Lymphocyte antigen 6E is a protein that in humans is encoded by the LY6E gene. Increased expression of Ly6E is associated with poor survival outcome in multiple malignancies as determined by a survey of more than 130 published clinical studies of gene expression studies on cancer tissue samples and adjacent normal tissues. Ly6E is associated with drug resistance and tumor immune escape in breast cancer. Further research is required to validate Ly6E for translation research.
References
Further reading |
https://en.wikipedia.org/wiki/SMC3 | Structural maintenance of chromosomes protein 3 (SMC3) is a protein that in humans is encoded by the SMC3 gene. SMC3 is a subunit of the Cohesin complex which mediates sister chromatid cohesion, homologous recombination and DNA looping. Cohesin is formed of SMC3, SMC1, RAD21 and either SA1 or SA2. In humans, SMC3 is present in all cohesin complexes whereas there are multiple paralogs for the other subunits.
SMC3 is a member of the SMC protein family. Members of this family are key regulators of DNA repair, chromosome condensation and chromosome segregation.
Structure and interactions
The domain organisation of SMC proteins is evolutionarily conserved and is composed of an N-terminal Walker A motif, coiled-coil, "hinge", coiled-coil and a C-terminal Walker B motif. The protein folds back on itself to form a rod-shaped molecule with a heterodimerisation "hinge" domain at one end and an ABC-type ATPase "head" at the other. These globular domains are separated by a ~50 nm anti-parallel coiled-coil. SMC3 and SMC1 bind via their hinge domains creating V-shaped heterodimers. The N-terminal domain of RAD21 binds to the coiled coil of SMC3 just above the head domain while the C-terminal domain of RAD21 binds the head domain of SMC1. This end to end binding of the SMC3-SMC1-RAD21 trimer creates a closed ring within which DNA can be entrapped. SA1 or
When DNA is replicated and sister chromatid cohesion is established SMC3 is acetylated on a pair of highly conserved lysines by ES |
https://en.wikipedia.org/wiki/PCSK7 | Proprotein convertase subtilisin/kexin type 7 is an enzyme that in humans is encoded by the PCSK7 gene.
The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine endoprotease. It is structurally related to its family members, PACE and PACE4. This protein is concentrated in the trans-Golgi network, associated with the membranes, and is not secreted. It can process proalbumin and is thought to be responsible for the activation of HIV envelope glycoproteins gp160 and gp140.
This gene has been implicated in the transcriptional regulation of housekeeping genes. Multiple alternatively spliced transcripts are described for this gene but their full length nature is not yet known. Downstream of this gene's map location at 11q23-q24, nucleotides that match part of this gene's 3' end are duplicated and inverted. A translocation breakpoint associated with lymphoma occurs between this gene and its inverted counterpart.
References
Further reading |
https://en.wikipedia.org/wiki/MTA2 | Metastasis-associated protein MTA2 is a protein that in humans is encoded by the MTA2 gene.
MTA2 is the second member of the MTA family of genes. MTA2 protein localizes in the nucleus and is a component of the nucleosome remodeling and the deacetylation complex (NuRD). Similar to the founding family member MTA1, MTA2 functions as a chromatin remodeling factor and regulates gene expression. MTA2 is overexpressed in human cancer and its dysregulated level correlates well with cancer invasiveness and aggressive phenotypes.
Discovery
MTA2 was initially recognized as an MTA1 like 1 gene, named MTA1-L1, from a large scale sequencing of randomly selected clones from human cDNA libraries in 1999. Clues about the role of MTA2 in gene expression came from the association of MTA2 polypeptides in the NuRD complex in a proteomic study This was followed by targeted cloning of murine Mta2 in 2001.
Gene and spliced variants
MTA2 is localized on chromosome 11q12-q13.1 in human and on 19B in mice. The 8.6-kb long human MTA2 gene contains 20 exons and seven transcripts inclusive of three protein-coding transcripts but predicted to code for two polypeptides of 688 amino acids and 495 amino acids. The remaining four MTA2 transcripts are non-coding RNA transcripts ranging from 532-bp to 627-bp. The murine Mta2 consists of a 3.1-kb protein-coding transcript to code a protein of 668 amino acids, and five non-coding RNAs transcripts, ranging from 620-bp to 839-bp.
Structure
Amino acid sequ |
https://en.wikipedia.org/wiki/VAMP3 | Vesicle-associated membrane protein 3 is a protein that in humans is encoded by the VAMP3 gene.
Function
Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Because of its high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, the protein encoded by this gene was shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.
Interactions
VAMP3 has been shown to interact with
BCAP31,
BVES,
SNAP23,
STX4,
STX6.
References
Further reading |
https://en.wikipedia.org/wiki/MED21 | Mediator of RNA polymerase II transcription subunit 21 is an enzyme that in humans is encoded by the MED21 gene.
Interactions
MED21 has been shown to interact with:
BRCA1,
CDK8,
GTF2F1,
GTF2H4,
MED6, and
POLR2A.
References
Further reading |
https://en.wikipedia.org/wiki/CRSP3 | Mediator of RNA polymerase II transcription subunit 23 is an enzyme that in humans is encoded by the MED23 gene.
Function
The activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The protein encoded by this gene is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. This protein also acts as a metastasis suppressor. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.
Interactions
CRSP3 has been shown to interact with Estrogen receptor alpha, CEBPB and Cyclin-dependent kinase 8.
References
External links
Further reading |
https://en.wikipedia.org/wiki/ATG5 | Autophagy related 5 (ATG5) is a protein that, in humans, is encoded by the ATG5 gene located on Chromosome 6. It is an E3 ubi autophagic cell death. ATG5 is a key protein involved in the extension of the phagophoric membrane in autophagic vesicles. It is activated by ATG7 and forms a complex with ATG12 and ATG16L1. This complex is necessary for LC3-I (microtubule-associated proteins 1A/1B light chain 3B) conjugation to PE (phosphatidylethanolamine) to form LC3-II (LC3-phosphatidylethanolamine conjugate). ATG5 can also act as a pro-apoptotic molecule targeted to the mitochondria. Under low levels of DNA damage, ATG5 can translocate to the nucleus and interact with survivin.
ATG5 is known to be regulated via various stress induced transcription factors and protein kinases.
Structure
ATG5 comprises three domains: a ubiquitin-like N-terminal domain (UblA), a helix-rich domain (HR) and a ubiquitin-like C-terminal domain (UblB). The three domains are connected by two linker regions (L1 and L2). ATG5 also has an alpha-helix at the N terminus where on Lysine 130 conjugation with ATG12 occurs. Both UblA and UbLB are composed of a five-stranded beta-sheet and two alpha-helices, a feature conserved in most ubiquitin and ubiquitin-like proteins. HR is composed of three long and one short alpha helices, forming a helix-bundle structure.
Regulation
ATG5 is regulated by the p73 from the p53 family of transcription factors. DNA damage induces the p300 acetylase to acetylate p73 with |
https://en.wikipedia.org/wiki/RNF7 | RING-box protein 2 is a protein that in humans is encoded by the RNF7 gene.
The protein encoded by this gene is a highly conserved ring finger protein. It is an essential subunit of SKP1-cullin/CDC53-F box protein ubiquitin ligases, which are a part of the protein degradation machinery important for cell cycle progression and signal transduction. This protein interacts with, and is a substrate of, casein kinase II (CSNK2A1/CKII). The phosphorylation of this protein by CSNK2A1 has been shown to promote the degradation of IkappaBalpha (CHUK/IKK-alpha/IKBKA) and p27Kip1(CDKN1B). Alternatively spliced transcript variants encoding distinct isoforms have been reported.
Interactions
RNF7 has been shown to interact with CSNK2B.
See also
RING finger domain
References
Further reading
External links
RING finger proteins |
https://en.wikipedia.org/wiki/TOMM20 | Mitochondrial import receptor subunit TOM20 homolog is a protein that in humans is encoded by the TOMM20 gene. TOM20 is one of the receptor systems of the TOM complex (translocase of the outer membrane) in the outer mitochondrial membrane (OMM).
Function
In mitochondrial protein import, TOM20 is closely associated with the pore-forming TOM40 complex and acts by recognizing and binding the N-terminal MTSs (matrix-targeting sequences), which form an amphipathic alpha helix and aid passage of the target proteins into the mitochondrial matrix.
See also
Mitochondria Outer Membrane Translocase
TOMM22
TOMM40
TOMM70A
References
Further reading |
https://en.wikipedia.org/wiki/ZBTB33 | Transcriptional regulator Kaiso is a protein that in humans is encoded by the ZBTB33 gene. This gene encodes a transcriptional regulator with bimodal DNA-binding specificity, which binds to methylated CGCG and also to the non-methylated consensus KAISO-binding site TCCTGCNA. The protein contains an N-terminal POZ/BTB domain and 3 C-terminal zinc finger motifs. It recruits the N-CoR repressor complex to promote histone deacetylation and the formation of repressive chromatin structures in target gene promoters. It may contribute to the repression of target genes of the Wnt signaling pathway, and may also activate transcription of a subset of target genes by the recruitment of catenin delta-2 (CTNND2). Its interaction with catenin delta-1 (CTNND1) inhibits binding to both methylated and non-methylated DNA. It also interacts directly with the nuclear import receptor Importin-α2 (also known as karyopherin alpha2 or RAG cohort 1), which may mediate nuclear import of this protein. Alternatively spliced transcript variants encoding the same protein have been identified.
NAMED by Dr.Juliet Daniel's, the KAISO gene was named after 'calypso' music popular in the Caribbeans, Trinidad & Tobago, e.t.c.
Interactions
ZBTB33 has been shown to interact with HDAC3, Nuclear receptor co-repressor 1 and CTNND1.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/DNAJB6 | DnaJ homolog subfamily B member 6 is a protein that in humans is encoded by the DNAJB6 gene.
Function
This gene encodes a member of the DNAJ protein family. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. This family member may also play a role in polyglutamine aggregation in specific neurons. Alternative splicing of this gene results in multiple transcript variants; however, not all variants have been fully described.
Interactions
DNAJB6 has been shown to interact with keratin 18. It has been also shown that the aggregation of Aβ42 (a process involved in e.g. Alzheimer's disease) is retarded by DNAJB6 in a concentration-dependent manner, extending to very low sub-stoichiometric molar ratios of chaperone to peptide. Dominant mutations in DNAJB6 have also been found to cause a late-onset muscle disease termed limb-girdle muscular dystrophy type D1 (LGMDD1), which is characterized by protein aggregation and vacuolar myopathology.
References
Further reading
External links
Heat shock proteins
Co-chaperones |
https://en.wikipedia.org/wiki/HUWE1 | E3 ubiquitin-protein ligase HUWE1 is an enzyme that in humans is encoded by the HUWE1 gene.
It performs the third step (ligation) in binding ubiquitin to proteins in a process called ubiquitination which tags the proteins for disposal.
Human genetic studies that implicate HUWE1 in intellectual disability. Additional research suggests HUWE1 has implications in cancer research.
References
Further reading
External links
International HUWE1 Community: www.huwe1.org
Louie's HUWE - a US 501c3 nonprofit to support people with HUWE1-related genetic conditions: www.huwe1.org/louieshuwe |
https://en.wikipedia.org/wiki/InaD-like%20protein | InaD-like protein is a protein that in humans is encoded by the PATJ gene.
Function
This gene encodes a protein with multiple PDZ domains. PDZ domains mediate protein-protein interactions, and proteins with multiple PDZ domains often organize multimeric complexes at the plasma membrane. This protein localizes to tight junctions and to the apical membrane of epithelial cells. A similar protein in Drosophila is a scaffolding protein which tethers several members of a multimeric signaling complex in photoreceptors.
Interactions
INADL has been shown to interact with MPP5.
References
Further reading
External links |
https://en.wikipedia.org/wiki/OLIG2 | Oligodendrocyte transcription factor (OLIG2) is a basic helix-loop-helix (bHLH) transcription factor encoded by the OLIG2 gene. The protein is of 329 amino acids in length, 32 kDa in size and contains one basic helix-loop-helix DNA-binding domain. It is one of the three members of the bHLH family. The other two members are OLIG1 and OLIG3. The expression of OLIG2 is mostly restricted in central nervous system, where it acts as both an anti-neurigenic and a neurigenic factor at different stages of development. OLIG2 is well known for determining motor neuron and oligodendrocyte differentiation, as well as its role in sustaining replication in early development. It is mainly involved in diseases such as brain tumor and Down syndrome.
Function
OLIG2 is mostly expressed in restricted domains of the brain and spinal cord ventricular zone which give rise to oligodendrocytes and specific types of neurons. In the spinal cord, the pMN region sequentially generates motor neurons and oligodendrocytes. During embryogenesis, OLIG2 first directs motor neuron fate by establishing a ventral domain of motor neuron progenitors and promoting neuronal differentiation. OLIG2 then switches to promoting the formation of oligodendrocyte precursors and oligodendrocyte differentiation at later stages of development. Apart from functioning as a neurogenic factor in specification and the differentiation of motor neurons and oligodendrocytes, OLIG2 also functions as an anti-neurogenic factor at early t |
https://en.wikipedia.org/wiki/Aldo-keto%20reductase%20family%201%2C%20member%20A1 | Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. AKR1A1 belongs to the aldo-keto reductase (AKR) superfamily. It catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols and catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Mutations in the AKR1A1 gene has been found associated with non-Hodgkin's lymphoma.
Structure
Gene
The AKR1A1 gene lies on the chromosome location of 1p34.1 and consists of 10 exons.
Protein
AKR1A1 consists of 325 amino acids and weighs 36573Da. The tertiary structure consists of a beta/alpha-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel. Alternative splicing of this gene results in two transcript variants encoding the same protein.
Function
AKR1A1 gene is found highly expressed in kidney and liver, and moderately expressed in cerebrum, small intestine and testis. Small amounts of AKR1A1 are present in lung, prostate and spleen. However, it is not observed in heart or skeletal muscle. AKR1A1 belongs to the AKR superfamily, which are predominantly monomeric, soluble, NADPH-dependent oxidoreductases involved in the reduction of aldehydes and ketones into primary and secondary alcohols. AKR1A1 is shown to demonstrate characteristically high specific activity towards many aromatic |
https://en.wikipedia.org/wiki/CUGBP2 | CUGBP, Elav-like family member 2, also known as Etr-3 is a protein that in humans is encoded by the CELF2 gene.
Members of the CELF/BRUNOL protein family are RNA-binding proteins and contain two N-terminal RNA recognition motif (RRM) domains, one C-terminal RRM domain, and a divergent segment of 160-230 aa between the second and third RRM domains. Members of this protein family regulate pre-mRNA alternative splicing and may also be involved in mRNA editing, and translation. Alternative splicing results in multiple transcript variants encoding different isoforms.
Interactions
CUGBP2 has been shown to interact with A1CF.
References
External links
Further reading |
https://en.wikipedia.org/wiki/NUDC | Nuclear migration protein nudC is a protein that in humans is encoded by the NUDC gene.
Interactions
NUDC has been shown to interact with PLK1 and PAFAH1B1.
References
Further reading |
https://en.wikipedia.org/wiki/HSPH1 | Heat shock protein 105 kDa is a protein that in humans is encoded by the HSPH1 gene.
Interactions
HSPH1 has been shown to interact with Cofilin 1.
References
Further reading |
https://en.wikipedia.org/wiki/Transcription%20elongation%20regulator%201 | Transcription elongation regulator 1, also known as TCERG1, is a protein which in humans is encoded by the TCERG1 gene.
Function
This gene encodes a nuclear protein that regulates transcriptional elongation and pre-mRNA splicing. The encoded protein interacts with the hyperphosphorylated C-terminal domain of RNA polymerase II via multiple FF domains, and with the pre-mRNA splicing factor SF1 via a WW domain. Alternative splicing results in multiple transcripts variants encoding different isoforms.
Interactions
Transcription elongation regulator 1 has been shown to interact with SF1 and POLR2A.
References
Further reading |
https://en.wikipedia.org/wiki/COPS8 | COP9 signalosome complex subunit 8 is a protein that in humans is encoded by the COPS8 gene.
The protein encoded by this gene is the smallest of the eight subunits of COP9 signalosome, a highly conserved protein complex that functions as an important regulator in multiple signaling pathways. The structure and function of COP9 signalosome is related to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome has been shown to interact with SCF-type E3 ubiquitin ligases and act as a positive regulator of E3 ubiquitin ligases. Alternatively spliced transcript variants encoding distinct isoforms have been observed.
References
External links
Further reading |
https://en.wikipedia.org/wiki/SF3B2 | Splicing factor 3B subunit 2 is a protein that in humans is encoded by the SF3B2 gene.
Function
This gene encodes subunit 2 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex binds pre-mRNA upstream of the intron's branch site in a sequence-independent manner and may anchor the U2 snRNP to the pre-mRNA. Splicing factor 3b is also a component of the minor U12-type spliceosome. Subunit 2 associates with pre-mRNA upstream of the branch site at the anchoring site. Subunit 2 also interacts directly with subunit 4 of the splicing factor 3b complex. Subunit 2 is a highly hydrophilic protein with a proline-rich N-terminus and a glutamate-rich stretch in the C-terminus.
Interactions
SF3B2 has been shown to interact with SF3B4, RBM7, SF3B1 and CDC5L.
References
Further reading |
https://en.wikipedia.org/wiki/LEKTI | Lympho-epithelial Kazal-type-related inhibitor (LEKTI) also known as serine protease inhibitor Kazal-type 5 (SPINK5) is a protein that in humans is encoded by the SPINK5 gene.
Structure and function
LEKTI is a large multidomain serine protease inhibitor expressed in stratified epithelial tissue. It consists of 15 domains that are cleaved into smaller, functional fragments by the protease furin. Only two of these domains (2 and 15) contain 6 evenly spaced cysteines responsible for 3 intramolecular disulfide bonds characteristic of Kazal-type related inhibitors. The remaining domains contain 4 cysteines. These disulfide bonds force the molecule into a rigid conformation that enables the protein to interact with a target protease via an extended beta-sheet. All domains (excepting 1, 2 and 15) contain an arginine at P1, indicating trypsin-like proteases are the likely targets.
In the epidermis, LEKTI is implicated in the regulation of desquamation via its ability to selectively inhibit KLK5, KLK7 and KLK14. Recombinant full length LEKTI inhibits the exogenous serine proteases trypsin, plasmin, subtilisin A, cathepsin G and human neutrophil elastase.
LEKTI may play a role in skin and hair morphogenesis and anti-inflammatory and/or antimicrobial protection of mucous epithelia.
Gene
SPINK5 is a member of a gene family cluster located on chromosome 5q32, which encode inhibitors of serine proteases. This includes other epidermal proteins SPINK6 and LEKTI-2 (SPINK9). The SPINK5 |
https://en.wikipedia.org/wiki/Centaurin%2C%20alpha%201 | Arf-GAP with dual PH domain-containing protein 1 is a protein that in humans is encoded by the ADAP1 gene.
Interactions
Centaurin, alpha 1 has been shown to interact with:
Casein kinase 1, alpha 1
Nucleolin,
P110α,
PRKCI,
Protein kinase D1, and
Protein kinase Mζ.
Model organisms
Model organisms have been used in the study of ADAP1 function. A conditional knockout mouse line called Adap1tm1a(EUCOMM)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
in-depth bone and cartilage phenotyping
References
Further reading
Proteins |
https://en.wikipedia.org/wiki/WWP1 | NEDD4-like E3 ubiquitin-protein ligase WWP1 is an enzyme that in humans is encoded by the WWP1 gene.
Function
WW domain-containing proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. This gene encodes a protein which contains 4 tandem WW domains and a HECT (homologous to the E6-associated protein carboxyl terminus) domain. The encoded protein belongs to a family of NEDD4-like proteins, which are E3 ubiquitin-ligase molecules and regulate key trafficking decisions, including targeting of proteins to proteosomes or lysosomes. Alternative splicing of this gene generates at least 6 transcript variants; however, the full length nature of these transcripts has not been defined. In neurons, murine ortholog Wwp1 and its homolog Wwp2 control polarity acquisition, formation, and branching of axons, as well as migration of newly born nerve cells into the cortical plate.
Interactions
WWP1 has been shown to interact with:
CPSF6,
KLF2, and
Reticulon 4
References
Further reading |
https://en.wikipedia.org/wiki/HNRPUL1 | Heterogeneous nuclear ribonucleoprotein U-like protein 1 is a protein that in humans is encoded by the HNRNPUL1 gene.
This gene encodes a nuclear RNA-binding protein of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. This protein binds specifically to adenovirus E1B-55kDa oncoprotein. It may play an important role in nucleocytoplasmic RNA transport, and its function is modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signalling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. Additional variants have also been found, but their full-length natures have not been determined.
Interactions
HNRPUL1 has been shown to interact with BRD7 and PRMT2.
References
Further reading |
https://en.wikipedia.org/wiki/Perilipin-2 | Adipose differentiation-related protein, also known as perilipin 2, ADRP or adipophilin, is a protein which belongs to the perilipin (PAT) family of cytoplasmic lipid droplet (CLD)–binding proteins. In humans it is encoded by the ADFP gene. This protein surrounds the lipid droplet along with phospholipids and is involved in assisting the storage of neutral lipids within the lipid droplets.
Discovery
The adipose differentiation related protein (ADRP) was first characterized as an mRNA molecule that express early in adipocyte differentiation. The full length cDNA was cloned by rapid amplification of cDNA ends method and sequence analysis results in a protein with 425 amino acids that is unique and similar sequences had not previously been reported.
Gene location
In humans, the gene for adipose differentiation related protein is located at short p arm of chromosome 9 at region 22 band 1 from base pair 19108391 to 19127606 (GRCh38.p7) (map).
Protein structure
The proposed models for adipose differentiation related protein (perilipin 2) is maintained by the protein model portal. It is based on homology modelling and no models were found with greater than 90 percent homology. Perlipin 2 has three different functional domains . 1-115 amino acid sequences at N-terminal is highly similar with other perlipin family proteins and is required for stabilization of lipid droplets, 103-215 mid- region is needed for binding at lipid droplets while the C-terminal sequence from 220- |
https://en.wikipedia.org/wiki/Chimerin%202 | Chimerin 2 (beta-chimaerin) is a protein that in humans is encoded by the CHN2 gene.
This gene is a member of the chimerin family and encodes a protein with a phorbol-ester/diacylglycerol-type zinc finger, a Rho-GAP domain and an SH2 domain. This protein has GTPase-activating protein activity that is regulated by phospholipid binding and binding of diacylglycerol (DAG) induces translocation of the protein from the cytosol to the Golgi apparatus membrane. The protein plays a role in the proliferation and migration of smooth muscle cells. Decreased expression of this gene is associated with high-grade gliomas and breast tumors, and increased expression of this gene is associated with lymphomas. Mutations in this gene have been associated with schizophrenia in men. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
References
Further reading |
https://en.wikipedia.org/wiki/CLCN2 | Chloride channel protein 2 is a protein that in humans is encoded by the CLCN2 gene. Mutations of this gene have been found to cause leukoencephalopathy and Idiopathic generalised epilepsy (), although the latter claim has been disputed. CLCN2 contains a transmembrane region that is involved in chloride ion transport as well two intracellular copies of the CBS domain.
See also
Chloride channel
References
Further reading
External links
Ion channels |
https://en.wikipedia.org/wiki/CLCN3 | H+/Cl− exchange transporter 3 is a protein that in humans is encoded by the CLCN3 gene.
Interactions
CLCN3 has been shown to interact with PDZK1.
See also
Chloride channel
References
Further reading
External links
Ion channels |
https://en.wikipedia.org/wiki/CLCN7 | Chloride channel 7 alpha subunit also known as H+/Cl− exchange transporter 7 is a protein that in humans is encoded by the CLCN7 gene. In melanocytic cells this gene is regulated by the Microphthalmia-associated transcription factor.
Clinical significance
Mutations in the CLCN7 gene have been reported to be associated with autosomal dominant osteopetrosis type II, a rare disease of bones.
See also
Chloride channel
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on CLCN7-Related Osteopetrosis
Ion channels |
https://en.wikipedia.org/wiki/CLCNKB | Chloride channel Kb, also known as CLCNKB, is a protein which in humans is encoded by the CLCNKB gene.
Chloride channel Kb (CLCNKB) is a member of the CLC family of voltage-gated chloride channels, which comprises at least 9 mammalian chloride channels. Each is believed to have 12 transmembrane domains and intracellular N and C termini. Mutations in CLCNKB result in the autosomal recessive Type III Bartter syndrome. CLCNKA and CLCNKB are closely related (94% sequence identity), tightly linked (separated by 11 kb of genomic sequence) and are both expressed in mammalian kidney.
See also
Chloride channel
BSND, barttin, accessory subunit beta for this channel
References
Further reading
External links
Ion channels |
https://en.wikipedia.org/wiki/CLK1 | Dual specificity protein kinase CLK1 is an enzyme that in humans is encoded by the CLK1 gene.
Function
This gene encodes a member of the CDC2-like (or LAMMER) family of dual specificity protein kinases. In the cell nucleus, the encoded protein phosphorylates serine/arginine-rich proteins involved in pre-mRNA processing, releasing them into the nucleoplasm. The choice of splice sites during pre-mRNA processing may be regulated by the concentration of transacting factors, including serine/arginine-rich proteins. Therefore, the encoded protein may play an indirect role in governing splice site selection.
Interactions
CLK1 has been shown to interact with ASF/SF2.
References
External links
Further reading |
https://en.wikipedia.org/wiki/HAPLN1 | Hyaluronan and proteoglycan link protein 1 is a protein that in humans is encoded by the HAPLN1 gene.
Interactions
HAPLN1 has been shown to interact with Versican.
References
Further reading
Extracellular matrix proteins
Glycoproteins |
https://en.wikipedia.org/wiki/CTBP2 | C-terminal-binding protein 2 also known as CtBP2 is a protein that in humans is encoded by the CTBP2 gene.
Function
The CtBPs - CtBP1 and CtBP2 in mammals - are among the best characterized transcriptional corepressors. They typically turn their target genes off. They do this by binding to sequence-specific DNA-binding proteins that carry a short motif of the general form Proline-Isoleucine-Aspartate-Leucine-Serine (the PIDLS motif). They then recruit histone modifying enzymes, histone deacetylases, histone methylases and histone demethylases. These enzymes are thought to work together to remove activating and add repressive histone marks. For example, histone deacetylase 1 (HDAC1) and HDAC2 can remove the activating mark histone 3 acetyl lysine 9 (H3K9Ac), then the histone methylase G9a can add methyl groups, while the histone demethylase lysine specific demethylase 1 (LSD1) can remove the activating mark H3K4me.
The CtBPs bind to many different DNA-binding proteins and also bind to co-repressors that are themselves bound to DNA-binding proteins, such as Friend of GATA (Fog). CtBPs can also dimerize and multimerize to bridge larger transcriptional complexes. They appear to be primarily scaffold proteins that allow the assembly of gene repression complexes.
One interesting aspect of CtBPs is their ability to bind to NADH and to a lesser extent NAD+. It has been proposed that this will enable them to sense the metabolic status of the cell and to regulate genes in response |
https://en.wikipedia.org/wiki/CYP4B1 | Cytochrome P450 4B1 is a protein that in humans is encoded by the CYP4B1 gene.
This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum. In rodents, the homologous protein has been shown to metabolize certain carcinogens; however, the specific function of the human protein has not been determined.
References
External links
Further reading |
https://en.wikipedia.org/wiki/DIAPH1 | Protein diaphanous homolog 1 is a protein that in humans is encoded by the DIAPH1 gene.
Function
This gene is a homolog of the Drosophila diaphanous gene and belongs to the protein family of the formins, characterized by the formin homology 2 (FH2) domain. It has been linked to autosomal dominant, fully penetrant, nonsyndromic low-frequency progressive sensorineural hearing loss. Actin polymerization involves proteins known to interact with diaphanous protein in Drosophila and mouse. It has therefore been speculated that this gene may have a role in the regulation of actin polymerization in hair cells of the inner ear. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
Interactions
DIAPH1 has been shown to interact with RHOA.
Clinical significance
Mutations in this gene have been associated with macrothrombocytopenia and hearing loss, microcephaly, blindness, and early onset seizures
Its actions on platelet formation appear to occur at the level of the megakaryocyte where it is involved in cytoskeleton formation.
See also
mDia1
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Deafness and Hereditary Hearing Loss Overview
DIAPH1 Info with links in the Cell Migration Gateway |
https://en.wikipedia.org/wiki/DLX5 | Homeobox protein DLX-5 is a protein that in humans is encoded by the distal-less homeobox 5 gene, or DLX5 gene. DLX5 is a member of DLX gene family.
Function
This gene encodes a member of a homeobox transcription factor gene family similar to the Drosophila distal-less (Dll) gene. The encoded protein may play a role in bone development and fracture healing. Current research holds that the homeobox gene family is important in appendage development. DLX5 and DLX6 can be seen to work in conjunction and are both necessary for proper craniofacial, axial, and appendicular skeleton development. Mutation in this gene, which is located in a tail-to-tail configuration with another member of the family on the long arm of chromosome 7, may be associated with split-hand/split-foot malformation.
DLX5 also acts as the early BMP-responsive transcriptional activator needed for osteoblast differentiation by stimulating the up-regulation of a variety of promoters (ALPL promoter, SP7 promoter, MYC promoter).
Clinical significance
Mutations in the DLX5 gene have been shown to be involved in the hand and foot malformation syndrome. SHFM is a heterogenous limb defect in which the development of the central digital rays is hindered, leading to missing central digits and claw-like distal extremities. Other defects associated with DLX5 include sensorineural hearing loss, mental retardation, ectodermal and craniofacial findings, and orofacial clefting.
In mice, the targeted disruption of DLX1, |
https://en.wikipedia.org/wiki/DUT%20%28gene%29 | DUTP pyrophosphatase, also known as DUT, is an enzyme which in humans is encoded by the DUT gene on chromosome 15.
This gene encodes an essential enzyme of nucleotide metabolism. The encoded protein forms a ubiquitous, homotrimeric enzyme that hydrolyzes dUTP to dUMP and pyrophosphate. This reaction serves two cellular purposes: providing a precursor (dUMP) for the synthesis of thymine nucleotides needed for DNA replication, and limiting intracellular pools of dUTP. Elevated levels of dUTP lead to increased incorporation of uracil into DNA, which induces extensive excision repair mediated by uracil glycosylase. This repair process, resulting in the removal and reincorporation of dUTP, is self-defeating and leads to DNA fragmentation and cell death. Alternative splicing of this gene leads to different isoforms that localize to either the mitochondrion or nucleus. A related pseudogene is located on chromosome 19.
Structure
In humans, this gene encodes a homotrimeric enzyme with two isoforms characterized by their distinct subcellular localizations: the nuclear isoform (DUT-N) and mitochondrial isoform (DUT-M).
Gene
Northern blot analysis reveals distinct mRNA transcripts for DUT-N (1.1 kb) and DUT-M (1.4 kb). The isoforms are produced from alternative splicing at different 5' exons, with the first exon of DUT-N occurring 767 base pairs downstream of the first exon in DUT-M. Regulation at different promoters has been proposed to account for the differential expression of |
https://en.wikipedia.org/wiki/Ephrin%20A4 | Ephrin A4 is a protein that in humans is encoded by the EFNA4 gene.
This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. This gene encodes an EFNA class ephrin. Three transcript variants that encode distinct proteins have been identified.
References
Further reading |
https://en.wikipedia.org/wiki/ERN1 | The serine/threonine-protein kinase/endoribonuclease inositol-requiring enzyme 1 α (IRE1α) is an enzyme that in humans is encoded by the ERN1 gene.
Function
The protein encoded by this gene is the ER to nucleus signalling 1 protein, a human homologue of the yeast Ire1 gene product. This protein possesses intrinsic kinase activity and an endoribonuclease activity and it is important in altering gene expression as a response to endoplasmic reticulum-based stress signals (mainly the unfolded protein response). Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Signaling
IRE1α possesses two functional enzymatic domains, an endonuclease and a trans-autophosphorylation kinase domain. Upon activation, IRE1α oligomerizes and carries out an unconventional RNA splicing activity, removing an intron from the X-box binding protein 1 (XBP1) mRNA, and allowing it to become translated into a functional transcription factor, XBP1s. XBP1s upregulates ER chaperones and endoplasmic reticulum associated degradation (ERAD) genes that facilitate recovery from ER stress.
Clinical significance
As IRE1α is a primary sensor for unfolded protein response, its disruption could be linked with neurodegenerative diseases, by which the accumulation of intracellular toxic proteins serves as one of the key pathogenic mechanisms. IRE1 signalling is considered to be pathogenic in Alzheimer's disease, Parkinson's disease and amyotrophic lateral scleros |
https://en.wikipedia.org/wiki/BPTF | Nucleosome-remodeling factor subunit BPTF is a protein that in humans is encoded by the BPTF gene.
This gene was identified by the reactivity of its encoded protein to a monoclonal antibody prepared against brain homogenates from patients with Alzheimer's disease. Analysis of the original protein (fetal Alz-50 reactive clone 1, or FAC1), identified as an 810 aa protein containing a DNA-binding domain and a zinc finger motif, suggested it might play a role in the regulation of transcription. High levels of FAC1 were detected in fetal brain and in patients with neurodegenerative diseases. The protein encoded by this gene is actually much larger than originally thought, and it also contains a C-terminal bromodomain characteristic of proteins that regulate transcription during proliferation. The encoded protein is highly similar to the largest subunit of the Drosophila NURF (nucleosome remodeling factor) complex. In Drosophila, the NURF complex, which catalyzes nucleosome sliding on DNA and interacts with sequence-specific transcription factors, is necessary for the chromatin remodeling required for transcription. Two alternative transcripts encoding different isoforms have been described completely.
Interactions
BPTF has been shown to interact with MAZ.
References
External links
Further reading |
https://en.wikipedia.org/wiki/EFEMP1 | EGF-containing fibulin-like extracellular matrix protein 1 is a protein that in humans is encoded by the EFEMP1 gene.
Gene
This gene encodes a member of the fibulin family of extracellular matrix glycoproteins. Like all members of this family, the encoded protein contains tandemly repeated epidermal growth factor-like repeats followed by a C-terminus fibulin-type domain. This gene is upregulated in malignant gliomas and may play a role in the aggressive nature of these tumors. Mutations in this gene are associated with Doyne honeycomb retinal dystrophy and with predisposition to hernias. Alternatively spliced transcript variants that encode the same protein have been described.[provided by RefSeq, Nov 2009]. This gene spans approximately 18 kb of genomic DNA and consists of 12 exons. Alternative splice patterns in the 5' UTR result in three transcript variants encoding the same extracellular matrix protein.
Clinical significance
Mutations in this gene are associated with Doyne honeycomb retinal dystrophy and with predisposition to hernias.
EFEMP1/Fibulin-3 has recently been reported as a potential biomarker to facilitate the identification of patients with pleural mesothelioma.
Interactions
EFEMP1 has been shown to interact with ARAF.
References
Further reading |
https://en.wikipedia.org/wiki/FGF4 | Fibroblast growth factor 4 is a protein that in humans is encoded by the FGF4 gene.
The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This gene was identified by its oncogenic transforming activity. This gene and FGF3, another oncogenic growth factor, are located closely on chromosome 11. Co-amplification of both genes was found in various kinds of human tumors. Studies on the mouse homolog suggested a function in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway.
Function
During embryonic development, the 21-kD protein FGF4 functions as a signaling molecule that is involved in many important processes. Studies using Fgf4 gene knockout mice showed developmental defects in embryos both in vivo and in vitro, revealing that FGF4 facilitates the survival and growth of the inner cell mass during the postimplantation phase of development by acting as an autocrine or paracrine ligand. FGFs produced in the apical ectodermal ridge (AER) are critical for the proper forelimb and hindlimb outgrowth. FGF signaling in the AER is involved in regulating limb digit number and cell death in the interdigital mesenchyme. When FGF signaling dynamics and regulatory processes are altered, |
https://en.wikipedia.org/wiki/FGF5 | Fibroblast growth factor 5 is a protein that in humans is encoded by the FGF5 gene.
The majority of FGF family members are glycosaminoglycan binding proteins which possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF proteins interact with a family of specific tyrosine kinase receptors, a process often regulated by proteoglycans or extracellular binding protein cofactors. A number of intracellular signalling cascades are known to be activated after FGF-FGFR interaction including PI3K-AKT, PLCγ, RAS-MAPK and STAT pathways.
Receptor
FGF5 is a 268 amino acid, 29.1 kDa protein, which also naturally occurs as a 123 amino acid isoform splice variant (FGF5s). FGF5 is produced in the outer root sheath of the hair follicle as well as perifollicular macrophages, with maximum expression occurring in the late anagen phase of the hair cycle. The receptor for FGF5, FGFR1, is largely expressed in the dermal papilla cells of the hair follicle. The alternatively spliced isoform FGF5s, has been identified as an antagonist of FGF5 in a number of studies.
Role in hair cycling
The only described function of FGF5 in adults is in the regulation of the hair cycle. FGF5 performs a critical role in the hair cycle, where it acts as the key signalling molecule in initiating the transition from the anagen (growth) phase to the catagen (regr |
https://en.wikipedia.org/wiki/FKBP1B | Peptidyl-prolyl cis-trans isomerase FKBP1B is an enzyme that in humans is encoded by the FKBP1B gene.
Function
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 (tacrolimus) and rapamycin (sirolimus). It is highly similar to the FK506-binding protein 1A. Its physiological role is thought to be in excitation-contraction coupling in cardiac muscle. There are two alternatively spliced transcript variants of this gene encoding different isoforms.
Clinical significance
Defective interaction between FKB1B and the ryanodine receptor is thought to be a potential mechanism underlying the arrhythmias seen in those with the genetic condition catecholaminergic polymorphic ventricular tachycardia.
References
Further reading
EC 5.2.1 |
https://en.wikipedia.org/wiki/STRAP | Serine-threonine kinase receptor-associated protein is an enzyme that in humans is encoded by the STRAP gene.
Interactions
STRAP has been shown to interact with:
Mothers against decapentaplegic homolog 2,
Mothers against decapentaplegic homolog 3,
Mothers against decapentaplegic homolog 6,
Mothers against decapentaplegic homolog 7,
TGF beta receptor 1, and
TGF beta receptor 2.
References
Further reading |
https://en.wikipedia.org/wiki/RRAS2 | Ras-related protein R-Ras2 is a protein that in humans is encoded by the RRAS2 gene.
Interactions
RRAS2 has been shown to interact with C-Raf.
References
Further reading |
https://en.wikipedia.org/wiki/COMMD1 | COMM domain-containing protein 1 is a protein that is encoded by the COMMD1 gene in humans. It was originally regarded as Murr1 before being differentiated and renamed by Dr. Ezra Burstein's Lab
References
External links
Further reading |
https://en.wikipedia.org/wiki/Annexin%20A7 | Annexin A7 is a protein that in humans is encoded by the ANXA7 gene.
Annexin VII is a member of the annexin family of calcium-dependent phospholipid binding proteins. The Annexin VII gene contains 14 exons and spans approximately 34 kb of DNA. An alternatively spliced cassette exon results in two mRNA transcripts of 2.0 and 2.4 kb which are predicted to generate two protein isoforms differing in their N-terminal domain. The alternative splicing event is tissue specific and the mRNA containing the cassette exon is prevalent in brain, heart and skeletal muscle. The transcripts also differ in their 3'-non coding regions by the use of two alternative poly(A) signals. The selection of poly(A) signals is independent of the mRNA splicing pattern. ~Annexin VII encodes a protein with a molecular weight of approximately 51 kDa with a unique, highly hydrophobic N-terminal domain of 167 amino acids and a conserved C-terminal region of 299 amino acids. The latter domain is composed of alternating hydrophobic and hydrophilic segments. Structural analysis of the protein suggests that Annexin VII is a membrane binding protein with diverse properties including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion.
Interactions
ANXA7 has been shown to interact with ALG2 and SRI.
References
External links
Further reading |
https://en.wikipedia.org/wiki/Annexin%20A11 | Annexin A11 is a protein that in humans is encoded by the ANXA11 gene.
Function
This gene encodes a member of the annexin family, a group of calcium-dependent phospholipid-binding proteins. Annexins have unique N-terminal domains and conserved C-terminal domains, which contain the calcium-dependent phospholipid-binding sites. The encoded protein is a 56-kD antigen recognized by sera from patients with various autoimmune diseases. Transcript variants encoding the same isoform have been identified.
Interactions
ANXA11 has been shown to interact with PDCD6 and ALG2.
Clinical significance
It is shown that over-expression of the ANXA11 is involved in apoptotic alterations in schizophrenia and contribute to pathomechanisms of this disorder.
References
External links
Further reading |
https://en.wikipedia.org/wiki/FUT2 | Galactoside 2-alpha-L-fucosyltransferase 2 is an enzyme that in humans is encoded by the FUT2 gene. It affects the secretor status of ABO antigens.
Approximately 20% of Caucasians are non-secretors due to the G428A (rs601338) and C571T (rs492602?) nonsense mutations in FUT2 and therefore have strong although not absolute protection from the norovirus GII.4.
References
Further reading |
https://en.wikipedia.org/wiki/GBP1 | Interferon-induced guanylate-binding protein 1 is a protein that in humans is encoded by the GBP1 gene. It belongs to the dynamin superfamily of large GTPases.
Function
Guanylate binding protein expression is induced by interferon. Guanylate binding proteins are characterized by their ability to specifically bind guanine nucleotides (GMP, GDP, and GTP) and are distinguished from the GTP-binding proteins by the presence of 2 binding motifs rather than 3.
References
Further reading |
https://en.wikipedia.org/wiki/GLUDP5 | Glutamate dehydrogenase pseudogene 5, also known as GLUDP5, is a human gene.
References
Further reading
Pseudogenes |
https://en.wikipedia.org/wiki/GRIA4 | Glutamate receptor 4 is a protein that in humans is encoded by the GRIA4 gene.
This gene is a member of a family of L-glutamate-gated ion channels that mediate fast synaptic excitatory neurotransmission. These channels are also responsive to the glutamate agonist, alpha-amino-3-hydroxy-5-methyl-4-isoxazolpropionate (AMPA). Some haplotypes of this gene show a positive association with schizophrenia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. Like the other AMPA receptor subunits, GluA4 occurs as flip and flop spliced variant. In addition, GluA4 CTD long and short isoforms exist, and presumably an ATD-only isoform (433 aa).
Interactions
GRIA4 has been shown to interact with CACNG2, GRIP1, PICK1 and PRKCG.
RNA editing
Several ion channels and neurotransmitters receptors pre-mRNa are substrates for ADARs. This includes 5 subunits of the glutamate receptor ionotropic AMPA glutamate receptor subunits (Glur2, Glur3, Glur4) and Kainate receptor subunits (Glur5, Glur6). Glutamate-gated ion channels are made up of four subunits per channel. Their function is in the mediation of fast neurotransmission to the brain. The diversity of the subunits is determined, as well as RNA splicing, by RNA editing events of the individual subunits. This give rise to the necessary diversity of the receptors. GluR4 is a gene product of the GRIA4 gene, and its pre-mRNA is subject to RNA editing.
Type
A to I RNA editing is catalyzed by a |
https://en.wikipedia.org/wiki/HIST1H2AE | Histone H2A type 1-B/E is a protein that in humans is encoded by the HIST1H2AE gene.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4).
The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.
References
Further reading |
https://en.wikipedia.org/wiki/HIST1H2BD | Histone H2B type 1-D is a protein that in humans is encoded by the HIST1H2BD gene.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryote. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H2B family. Two transcripts that encode the same protein have been identified for this gene, which is found in the large histone gene cluster on chromosome 6p22-p21.3.
References
Further reading |
https://en.wikipedia.org/wiki/HIST1H1A | Histone H1.1 is a protein that in humans is encoded by the HIST1H1A gene.
Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H1 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.
References
Further reading |
https://en.wikipedia.org/wiki/HAS2 | Hyaluronan synthase 2 is an enzyme that in humans is encoded by the HAS2 gene.
Hyaluronan or hyaluronic acid is a high molecular weight unbranched polysaccharide synthesized by a wide variety of organisms from bacteria to mammals, and is a constituent of the extracellular matrix. It consists of alternating glucuronic acid and N-acetylglucosamine residues that are linked by beta-1-3 and beta-1-4 glycosidic bonds. Hyaluronic acid is synthesized by membrane-bound synthase at the inner surface of the plasma membrane, and the chains are extruded via ABC-Transporter into the extracellular space. It serves a variety of functions, including space filling, lubrication of joints, and provision of a matrix through which cells can migrate. Hyaluronic acid is produced during wound healing and tissue repair to provide a framework for ingrowth of blood vessels and fibroblasts. Changes in the serum concentration of hyaluronic acid are associated with inflammatory and degenerative arthropathies such as rheumatoid arthritis. In addition, the interaction of hyaluronic acid with the leukocyte receptor CD44 is important in tissue-specific homing by leukocytes, and overexpression of hyaluronic acid receptors has been correlated with tumor metastasis. HAS2 is a member of the vertebrate gene family encoding putative hyaluronan synthases, and its amino acid sequence shows significant homology to glycosaminoglycan synthetase (DG42) from Xenopus laevis, and human and murine hyaluronan synthase |
https://en.wikipedia.org/wiki/HNRNPL | Heterogeneous nuclear ribonucleoprotein L is a protein that in humans is encoded by the HNRNPL gene.
Function
Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogeneous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear ribonucleoprotein L is among the proteins that are stably associated with hnRNP complexes and along with other hnRNP proteins is likely to play a major role in the formation, packaging, processing, and function of mRNA. Heterogeneous nuclear ribonucleoprotein L is present in the nucleoplasm as part of the HNRP complex. HNRP proteins have also been identified outside of the nucleoplasm. Exchange of hnRNP for mRNA-binding proteins accompanies transport of mRNA from the nucleus to the cytoplasm. Since HNRP proteins have been shown to shuttle between the nucleus and the cytoplasm, it is possible that they also have cytoplasmic functions. Two transcript variants encoding different isoforms have been found for this gene.
Interactions
HNRNPL has been shown to interact with:
HNRNPLL,
HNRPK,
PCBP2, and
PTBP1.
References
Further reading |
https://en.wikipedia.org/wiki/TLX1 | T-cell leukemia homeobox protein 1 is a protein that in humans is encoded by the TLX1 gene, which was initially named HOX11.
Interactions
TLX1 has been shown to interact with PPP1CC, PPP2CB and PPP2CA.
References
Further reading |
https://en.wikipedia.org/wiki/HOXB1 | Homeobox protein Hox-B1 is a protein that in humans is encoded by the HOXB1 gene.
Function
This gene belongs to the homeobox family of genes. The homeobox genes encode a highly conserved family of transcription factors that play an important role in morphogenesis in all multicellular organisms. Mammals possess four similar homeobox gene clusters, HOXA, HOXB, HOXC and HOXD, located on different chromosomes, consisting of 9 to 11 genes arranged in tandem. This gene is one of several homeobox HOXB genes located in a cluster on chromosome 17.
Interactions
HOXB1 has been shown to interact with PBX1.
See also
Homeobox
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/HOXB2 | Homeobox protein Hox-B2 is a protein that in humans is encoded by the HOXB2 gene.
Function
This gene is a member of the Antp homeobox family and encodes a nuclear protein with a homeobox DNA-binding domain. It is included in a cluster of homeobox B genes located on chromosome 17. The encoded protein functions as a sequence-specific transcription factor that is involved in development. Increased expression of this gene is associated with pancreatic cancer.
See also
Homeobox
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/NLRP1 | NLRP1 encodes NACHT, LRR, FIIND, CARD domain and PYD domains-containing protein 1 in humans. NLRP1 was the first protein shown to form an inflammasome. NLRP1 is expressed by a variety of cell types, which are predominantly epithelial or hematopoietic. The expression is also seen within glandular epithelial structures including the lining of the small intestine, stomach, airway epithelia and in hairless or glabrous skin. NLRP1 polymorphisms are associated with skin extra-intestinal manifestations in CD. Its highest expression was detected in human skin, in psoriasis and in vitiligo. Polymorphisms of NLRP1 were found in lupus erythematosus and diabetes type 1. Variants of mouse NLRP1 were found to be activated upon N-terminal cleavage by the protease in anthrax lethal factor.
Function
This gene encodes a member of the Ced-4 family of apoptosis proteins. Ced-family members contain a caspase recruitment domain (CARD) and are known to be key mediators of programmed cell death. The encoded protein contains a distinct N-terminal pyrin-like motif, which is possibly involved in protein-protein interactions. The NLRP1 protein interacts strongly with caspase 2 and weakly with caspase 9. Overexpression of this gene was demonstrated to induce pyroptosis in cells. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene, but the biological validity of some variants has not been determined.
Mechanism of activation
NLRP1 activates an an |
https://en.wikipedia.org/wiki/MAPK8IP3 | C-jun-amino-terminal kinase-interacting protein 3 is an enzyme that in humans is encoded by the MAPK8IP3 gene.
The protein encoded by this gene shares similarity with the product of Drosophila syd gene, required for the functional interaction of kinesin I with axonal cargo. Studies of the similar gene in mouse suggested that this protein may interact with and regulate the activity of numerous protein kinases of the JNK signaling pathway, and thus function as a scaffold protein in neuronal cells. The C. elegans counterpart of this gene is found to regulate synaptic vesicle transport, possibly by integrating JNK signaling and kinesin-1 transport. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.
Interactions
MAPK8IP3 has been shown to interact with ASK1, C-Raf, PTK2, MAPK10, Mitogen-activated protein kinase 9, MAPK8, MAP2K1, KLC2, MAP2K7, KLC1, MAPK8IP2 and MAP2K4.
References
Further reading |
https://en.wikipedia.org/wiki/PRAME | PRAME (preferentially expressed antigen of melanoma) is a protein that in humans is encoded by the PRAME gene. Five alternatively spliced transcript variants encoding the same protein have been observed for this gene.
Function
This gene encodes an antigen that is predominantly expressed in human melanomas and that is recognized by cytolytic T lymphocytes. It is not expressed in normal tissues, except testis. This expression pattern is similar to that of other CT antigens, such as MAGE, BAGE and GAGE. However, unlike these other CT antigens, this gene is also expressed in acute leukemias. The overexpression of PRAME in tumor tissues and relative low levels in normal somatic tissues make it an attractive target for cancer therapy. In recent years, immunotherapy has spearheaded a new era of cancer therapy resulting in the development of numerous novel antigen-specific immunotherapy approaches. Studies on PRAME-specific immunotherapy primarily involve vaccines and cellular immunotherapies.
PRAME can inhibit retinoic acid signaling and retinoic acid mediated differentiation and apoptosis. PRAME overexpression in triple negative breast cancer has also been found to promote cancer cell motility through induction of the epithelial-to-mesenchymal transition.
Model organisms
Model organisms have been used in the study of PRAME function. A conditional knockout mouse line called Prametm1a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals under |
https://en.wikipedia.org/wiki/KIF4A | Kinesin family member 4A is a protein that in humans is encoded by the KIF4A gene.
Function
Kinesins, such as KIF4A, are microtubule-based motor proteins that generate directional movement along microtubules. They are involved in many crucial cellular processes, including cell division.
Interactions
KIF4A has been shown to interact with HMG20B and DNMT3B.
Clinical significance
NTCP is the entry receptor for both Hepatitis B (HBV) and Hepatitis D viruses (HDV). KIF4 was found to play an essential role in HBV and HDV infection through its regulation of the retrograde transport of NTCP from the cytoplasm to the cell surface where it acts as a receptor for HBV/HDV infection.
References
Further reading
External links
Human proteins
Motor proteins |
https://en.wikipedia.org/wiki/UNC84B | Protein unc-84 homolog B is a protein that in humans is encoded by the UNC84B gene.
References
Further reading |
https://en.wikipedia.org/wiki/ASF1A | Histone chaperone ASF1A is a protein that in humans is encoded by the ASF1A gene.
Function
This gene encodes a member of the H3/H4 family of histone chaperone proteins and is similar to the anti-silencing function-1 gene in yeast. The protein is a key component of a histone donor complex that functions in nucleosome assembly. It interacts with histones H3 and H4, and functions together with a chromatin assembly factor during DNA replication and repair.
Interactions
ASF1A has been shown to interact with TLK1, TLK2, CHAF1B and CHAF1A.
References
Further reading
External links |
https://en.wikipedia.org/wiki/GNL3 | Guanine nucleotide-binding protein-like 3, also known as nucleostemin, is a protein that in humans is encoded by the GNL3 gene. It is found within the nucleolus that binds p53. Nucleostemin regulates the cell cycle and affects cell differentiation, decreasing in amount as this differentiation progresses. It is a marker for many stem cells and cancer cells.
Interactions
GNL3 has been shown to interact with Mdm2 and P53.
References
Further reading |
https://en.wikipedia.org/wiki/SND1 | Staphylococcal nuclease domain-containing protein 1 also known as 100 kDa coactivator or Tudor domain-containing protein 11 (TDRD11) is a protein that in humans is encoded by the SND1 gene. SND1 is a main component of RISC complex and plays an important role in miRNA function. SND1 is Tudor domain containing protein and Tudor Proteins are highly conserved proteins and even present in Drosophila melanogaster. SND1 is also involved in Autism.
Clinical significance
SND1 acts as oncogene in many cancers and in hepatocellular carcinoma progression. SND1 promotes tumor angiogenesis in human hepatocellular carcinoma through a novel pathway which involves NF-kappaB and miR-221. SND1 promotes migration and invasion via angiotensin II type 1 receptor and TGFβ signaling. SND1 expression is regulated by Mir-184 in gliomas.
Interactions
SND1 has been shown to interact with MYB,
PIM1, POLR2A, RBPJ, and STAT6.
SND1 also interacts with G3BP (stress granule protein) and AEG-1.
References
Further reading |
https://en.wikipedia.org/wiki/TNRC6A | Trinucleotide repeat-containing gene 6A protein is a protein that in humans is encoded by the TNRC6A gene.
This gene encodes a member of the trinucleotide repeat containing 6 protein family. The protein functions in post-transcriptional gene silencing through the RNA interference (RNAi) and microRNA pathways. The protein associates with messenger RNAs and Argonaute proteins in cytoplasmic bodies known as GW-bodies or P-bodies. Inhibiting expression of this gene delocalizes other GW-body proteins and impairs RNAi and microRNA-induced gene silencing.
References
Further reading |
https://en.wikipedia.org/wiki/UHRF1 | Ubiquitin-like, containing PHD and RING finger domains, 1, also known as UHRF1, is a protein which in humans is encoded by the UHRF1 gene.
Function
This gene encodes a member of a subfamily of RING-finger type E3 ubiquitin ligases. The protein binds to hemi-methylated DNA during S-phase and recruits the main DNA methyltransferase protein, DNMT1, to regulate chromatin structure and gene expression. Its expression peaks at late G1 phase and continues during G2 and M phases of the cell cycle. It plays a major role in the G1/S transition, and functions in the p53-dependent DNA damage checkpoint. Multiple transcript variants encoding different isoforms have been found for this gene. It was originally identified as a direct regulator of topoisomerase 2a, but this has subsequently been disproven. Uhrf1 has been extensively studied in vivo using zebrafish.
Clinical significance
UHRF1 has recently been identified as a novel oncogene in hepatocellular carcinoma, the primary type of liver cancer.
References
Further reading |
https://en.wikipedia.org/wiki/ASPH | Aspartyl/asparaginyl beta-hydroxylase (HAAH) is an enzyme that in humans is encoded by the ASPH gene. ASPH is an alpha-ketoglutarate-dependent hydroxylase, a superfamily non-haem iron-containing proteins.
Function
This gene is thought to play an important role in calcium homeostasis. Alternative splicing of this gene results in five transcript variants which vary in protein translation, the coding of catalytic domains, and tissue expression. Variation among these transcripts impacts their functions which involve roles in the calcium storage and release process in the endoplasmic and sarcoplasmic reticulum as well as hydroxylation of aspartic acid and asparagine in epidermal growth factor-like domains of various proteins.
Clinical significance
As early as 1996, the over-expression of HAAH was recognized as an indicator of carcinoma in humans. Further research has correlated elevated HAAH levels (variously in affected tissue or blood serum) with hepatocellular (liver) carcinoma adenocarcinoma (pancreatic cancer), colorectal cancer, prostate cancer. and lung cancer. The pancreatic study showed elevated HAAH only in diseased tissue, but not in adjacent normal and inflamed tissue.
Mutations in ASPH cause Traboulsi syndrome.
References
External links
Further reading
Human 2OG oxygenases
EC 1.14.11 |
https://en.wikipedia.org/wiki/HOXB9 | Homeobox protein Hox-B9 is a protein that in humans is encoded by the HOXB9 gene.
Function
This gene is a member of the Abd-B homeobox family and encodes a protein with a homeobox DNA-binding domain. It is included in a cluster of homeobox B genes located on chromosome 17. The encoded nuclear protein functions as a sequence-specific transcription factor that is involved in cell proliferation and differentiation. Increased expression of this gene is associated with some cases of leukemia, prostate cancer and lung cancer.
Interactions
HOXB9 has been shown to interact with BTG2 and BTG1.
See also
Homeobox
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/HOXD3 | Homeobox protein Hox-D3 is a protein that in humans is encoded by the HOXD3 gene.
Function
This gene belongs to the homeobox family of genes. The homeobox genes encode a highly conserved family of transcription factors that play an important role in morphogenesis in all multicellular organisms. Mammals possess four similar homeobox gene clusters, HOXA, HOXB, HOXC and HOXD, located on different chromosomes, consisting of 9 to 11 genes arranged in tandem. This gene is one of several homeobox HOXD genes located at 2q31-2q37 chromosome regions. Deletions that removed the entire HOXD gene cluster or 5' end of this cluster have been associated with severe limb and genital abnormalities. The protein encoded by this gene may play a role in the regulation of cell adhesion processes.
See also
Homeobox
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/HSF2 | Heat shock factor protein 2 is a protein that in humans is encoded by the HSF2 gene.
Function
HSF2, as well as the related gene HSF1, encodes a protein that binds specifically to the heat-shock element and has homology to HSFs of other species. Heat shock transcription factors activate heat-shock response genes under conditions of heat or other stresses. Although the names HSF1 and HSF2 were chosen for historical reasons, these peptides should be referred to as heat-shock transcription factors.
Interactions
HSF2 has been shown to interact with Nucleoporin 62 and HSF1.
See also
Heat shock factor
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/IRF8 | Interferon regulatory factor 8 (IRF8) also known as interferon consensus sequence-binding protein (ICSBP), is a protein that in humans is encoded by the IRF8 gene. IRF8 is a transcription factor that plays critical roles in the regulation of lineage commitment and in myeloid cell maturation including the decision for a common myeloid progenitor (CMP) to differentiate into a monocyte precursor cell.
Function
Interferon Consensus Sequence-binding protein (ICSBP) is a transcription factor of the interferon regulatory factor (IRF) family. Proteins of this family are composed of a conserved DNA-binding domain in the N-terminal region and a divergent C-terminal region that serves as the regulatory domain. The IRF family proteins bind to the IFN-stimulated response element (ISRE) and regulate expression of genes stimulated by type I IFNs, namely IFN-α and IFN-β. IRF family proteins also control expression of IFN-α and IFN-β-regulated genes that are induced by viral infection.
Knockout studies
IFN-producing cells (mIPCs) were absent in all lymphoid organs from ICSBP knockout (KO) mice, as revealed by lack of CD11clowB220+Ly6C+CD11b− cells. In parallel, CD11c+ cells isolated from ICSBP KO spleens were unable to produce type I IFNs in response to viral stimulation. ICSBP KO mice also displayed a marked reduction of the DC subset expressing the CD8alpha marker (CD8alpha+ DCs) in spleen, lymph nodes, and thymus. Moreover, ICSBP-deficient CD8alpha+ DCs exhibited a markedly impaired ph |
https://en.wikipedia.org/wiki/IGHG1 | Ig gamma-1 chain C region is a protein that in humans is encoded by the IGHG1 gene.
References
Further reading |
https://en.wikipedia.org/wiki/Interleukin-9%20receptor | Interleukin 9 receptor (IL9R) also known as CD129 (Cluster of Differentiation 129) is a type I cytokine receptor. IL9R also denotes its human gene.
The protein encoded by this gene is a cytokine receptor that specifically mediates the biological effects of interleukin 9 (IL9). The functional IL9 receptor complex requires this protein as well as the interleukin 2 receptor, gamma (IL2RG), a common gamma subunit shared by the receptors of many different cytokines. The ligand binding of this receptor leads to the activation of various JAK kinases and STAT proteins, which connect to different biologic responses. This gene is located at the pseudoautosomal regions of X and Y chromosomes. Genetic studies suggested an association of this gene with the development of asthma. Multiple pseudogenes on chromosome 9, 10, 16, and 18 have been described. Alternatively spliced transcript variants encoding distinct isoforms have been reported.
Interactions
Interleukin-9 receptor has been shown to interact with YWHAZ.
See also
Cluster of differentiation
References
Further reading
External links
Type I cytokine receptors
Clusters of differentiation |
https://en.wikipedia.org/wiki/Interleukin%2010%20receptor%2C%20beta%20subunit | Interleukin 10 receptor, beta subunit is a subunit for the interleukin-10 receptor. IL10RB is its human gene.
IL10RB has also been designated CDw210b (cluster of differentiation w210b).
The protein encoded by this gene belongs to the cytokine receptor family. It is an accessory chain essential for the active interleukin 10 receptor complex. Coexpression of this and IL10RA proteins has been shown to be required for IL10-induced signal transduction. This gene and three other interferon receptor genes, IFNAR2, IFNAR1, and IFNGR2, form a class II cytokine receptor gene cluster located in a small region on chromosome 21.
References
Further reading
Clusters of differentiation
Type II cytokine receptors |
https://en.wikipedia.org/wiki/IL13RA2 | Interleukin-13 receptor subunit alpha-2 (IL-13Rα2), also known as CD213A2 (cluster of differentiation 213A2), is a membrane bound protein that in humans is encoded by the IL13RA2 gene.
Function
IL-13Rα2 is closely related to IL-13Rα1, a subunit of the interleukin-13 receptor complex. This protein binds IL13 with high affinity, but lacks any significant cytoplasmic domain, and does not appear to function as a signal mediator. It is, however, able to regulate the effects of both IL-13 and IL-4, despite the fact it is unable to bind directly to the latter. It is also reported to play a role in the internalization of IL13.
Clinical Significance
IL-13Rα2 has been found to be over-expressed in a variety of cancers, including pancreatic, ovarian, melanomas, and malignant gliomas.
See also
Interleukin-13 receptor
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/ILF2 | Interleukin enhancer-binding factor 2 is a protein that in humans is encoded by the ILF2 gene.
Function
Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of the interleukin 2 gene. NFAT binds to a sequence in the interleukin 2 gene enhancer known as the antigen receptor response element 2. In addition, NFAT can bind RNA and is an essential component for encapsidation and protein priming of hepatitis B viral polymerase. NFAT is a heterodimer of 45 kDa and 90 kDa proteins, the smaller of which is the product of this gene. The encoded protein binds strongly to the 90 kDa protein and stimulates its ability to enhance gene expression.
Interactions
ILF2 has been shown to interact with CDC5L and DNA-PKcs.
ILF2 and ILF3 have been identified as autoantigens in mice with induced lupus, in canine systemic rheumatic autoimmune disease, and as a rare finding in humans with autoimmune disease.
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Mouse Interleukin enhancer-binding factor 2 (ILF2)
Transcription factors |
https://en.wikipedia.org/wiki/KCNJ12 | ATP-sensitive inward rectifier potassium channel 12 is a lipid-gated ion channel that in humans is encoded by the KCNJ12 gene.
Function
This gene encodes an inwardly rectifying K+ channel that may be blocked by divalent cations. This protein is thought to be one of multiple inwardly rectifying channels that contribute to the cardiac inward rectifier current (IK1). The gene is located within the Smith–Magenis syndrome region on chromosome 17.
Interactions
KCNJ12 has been shown to interact with:
APBA1,
CASK,
DLG1,
DLG2,
DLG3,
DLG4,
LIN7A
LIN7B, and
LIN7C.
See also
Inward-rectifier potassium channel
References
Further reading
External links
Ion channels |
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