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Calumenin is a calcium-binding protein located in the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) of mammalian tissues which plays a role in ER functions as protein folding and sorting. Calumenin belongs to a family of multiple EF-hand proteins (CERC) that include reticulocalbin, ERC-55, and Cab45 and the product of this gene. Calumenin binds 7 calcium ions having low affinity and takes part in such ER functions as protein folding and sorting.

Calumenin is a calcium-binding protein located in the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) of mammalian tissues which plays a role in ER functions as protein folding and sorting. Calumenin belongs to a family of multiple EF-hand proteins (CERC) that include reticulocalbin, ERC-55, and Cab45 and the product of this gene. Calumenin binds 7 calcium ions having low affinity and takes part in such ER functions as protein folding and sorting.

Calmodulin (CaM) is an intracellular receptor protein for Ca2+-ions. It activates the myosin light chain kinase which is the catalyst of myosin phosphorylation. CaM participates in the activation of enzymes such as cyclic nucleotide- dependent phosphodiesterase, calcineurin, ATPase, Myosin Light Chain Kinases, and CAM kinase.

CALN1 is highly similar to the calcium-binding proteins of the calmodulin family. The CALN1 protein contains two EF-hand domains and potential calcium-binding sites. Also, CALN1 negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. CALN1 has a role in the physiology of neurons and is potentially significant in memory and learning.

Calmodulin-2 acts as an intracellular calcium sensor protein. When the intracellular Ca2+ concentration increases, calmodulin can bind up to four Ca2+, changing its conformation and regulating cellular functions such as activation or inhibition of a large number of enzymes, ion channels, and receptors. P53 protein stimulates CALM2 gene expression in 041 cells. CALM-2 is involved in the processes of Ca(2+)-induced neuronal cell death and the blockage of calmodulin attenuates brain injury after cerebral ischemia. Calmodulin-2 mediates the control of a large number of enzymes and other proteins by ca(2+). among the enzymes to be stimulated by the calmodulin-ca(2+) complex are a number of protein kinases and phosphatases.

Calmodulin Like 3 (CALML3) is a member of the calmodulin family and contains 4 EF-hand domains. The CALML3 protein may be similar to that of genuine calmodulin and may in fact compete with calmodulin by binding, with different affinities, to cellular substrates. CALML3 protein is expressed in normal mammary, prostate, cervical, and epidermal tissues.

Calmodulin Like 5, also known as CALML5 is a part of the calmodulin family of calcium binding proteins. CALML5 undergoes a conformational change as a result of binding calcium. CALML5 is taking part in terminal differentiation of keratinocytes and encodes a calcium binding protein expressed in the epidermis.

CAMLG binds to cyclophilin B and operates downstream of the TCR and upstream of calcineurin by causing an influx of calcium. CAMLG is an essential membrane protein that takes part in the calcium signal transduction pathway, connecting cyclophilin B to calcium signaling.

Sperm Antigen With Calponin Homology And Coiled-Coil 1 (SPECC1) which is a part of the cytospin-A family takes part in cytokinesis and spindle organization. SPECC1 takes part in actin cytoskeleton organization and microtubule stabilization and therefore necessary for proper cell adhesion and migration.

CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulin, troponin C and tropomyosin. Prevention of actomyosin Mg-ATPase activity is a result of interaction between calponin and actin.

Calcipressin-3 (RCAN3) takes part in central nervous system development. RCAN3 inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Overexpression of calcipressin-3 results in inhibition of calcineurin activity towards the nuclear factor of activated T-cells (NFAT) transcription factors and also downregulates NFAT-dependent cytokine gene expression in activated Jurkat T-cells. Highest expression takes place s in heart, skeletal muscle kidney, liver and peripheral blood leukocytes.

Calmodulin (CaM) is an intracellular receptor protein for Ca2+-ions. It activates the myosin light chain kinase which is the catalyst of myosin phosphorylation. CaM participates in the activation of enzymes such as cyclic nucleotide- dependent phosphodiesterase, calcineurin, ATPase, Myosin Light Chain Kinases, and CAM kinase.

RCAN2 is a member of the RCAN (Regulator of calcineurin) family that controls the activity of Calcineurin using a valine-rich region placed in their carboxyl tail. RCANs race against NFAT (nuclear factor of activated T-cells) to bind to the same docking site in calcineurin, and consequently inhibits or activates calcineurin activity. RCAN2 is a Ca(2+) dependent protein phosphatase which takes part in numerous neuornal functions.

Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).

Calponin 2 also known as CNN2 protein is capable of binding actin, calmodulin, troponin C, and tropomyosin, and also function in the structural organization of actin filaments. Furthermore, the interaction of CNN2 with actin inhibits the actomyosin Mg-ATPase activity. CNN2 takes part in smooth muscle contraction and cell adhesion. Two transcript variants encoding different isoforms have been found for this gene.

Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 2 (CAMK2N2) is a protein coding gene which regulates cell growth when overexpressed in colon adenocarcinoma LoVo cells. CAMK2N2 plays a role as a cellular inhibitor of CaM-kinase II (CAMK2).

Calbindin 1 (CALB1) is a calcium binding protein that is a member of the troponin C superfamily. CALB1 plays a vital role in calcium regulation (including calcium transport and uptake, calcification of bone and teeth) and calcium associated signaling in neurons and transiently in embryological development. CALB1 also has a role in protecting neurons from apoptotic cell death. CALB1 buffers cytosolic calcium and may stimulate a membrane Ca2+-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. The biological function of CALB1 seems to be tied to the redox state of its five cysteine residues.
CALB1 has 4 active calcium-binding domains, and 2 modified domains that seemingly have lost their calcium-binding ability. CALB1 is expressed in neural tissues. In the brain, the CALB1 synthesis is independent of vitamin-D-derived hormones.
Disregulation of the CALB1 is associated with epilepsy, amyotrophic lateral sclerosis, Huntington's disease. The neurons in brains of Huntington disease patients are calbindin-depleted.

Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.

Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.

Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).

Calbindins are Ca-binding proteins belonging to the troponin C superfamily. CALB28K/Calbindin1/CALB1 (D28K/Spot35 protein or cholecalcin, rat 261 aa; mouse 261 aa; human 261-aa, chromosome 8q21.3-q22.1) was originally described as 27-kDA induced by vitamin D in the duodenum of chicken. In mammals, it is expressed in the kidney, pancreatic islets, and brain. In brain, its synthesis is independent of vitamin D. CABP28K contains 4 active and 2 inactive EF-hand Ca-binding domains. The gene for CABP28K is clustered in the same region as carbonic anhydrase. The neurons in the brains of patients with Huntington disease are CAB28K depleted. There are two types of CaBPs: the "trigger"- and the "buffer"-CaBPs. The conformation of "trigger" type CaBPs changes upon Ca2+ binding and exposes regions on protein that interact with target molecules, thus altering their activity. The buffer-type CABP are thought to control the intracellular calcium concentration. Calbindin D-28K is found predominantly in subpopulations of central and peripheral nervous system neurons, and in certain epithelial cells involved in Ca2+ transport such as distal tubular cells and cortical collecting tubules of the kidney, and in enteric neuroendocrine cells.

S100A9 is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A9 protein is localized in the cytoplasm and/or nucleus of a wide range of cells, and participates in the regulation of several cellular processes such as cell cycle progression and differentiation. S100 genes include no less than 13 proteins which are localized as a cluster on chromosome 1q21. S100A9 is involved in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis.