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Dynein light chain roadblock-type (DYNLRB1) belongs to the roadblock dynein light chain family and encodes a cytoplasmic protein which is capable of binding intermediate chain proteins. Upregulation of the DYNLRB1 gene is linked with hepatocellular carcinomas, suggesting that DYNLRB1 may be involved in tumor progression.

Transcription elongation factor A protein-like 8 (TCEAL8) is a member of the TFS-II family and TFA subfamily. TCEAL8 is involved in transcriptional regulation and localized in nucleus. TFS-II family members contain TFA domains and act as nuclear phosphoproteins which control transcription in a promoter context-dependent mode. Numerous family members are found on the X chromosome.

Carbonic Anhydrase XIII, also known as CA13 is a member of the alpha-carbonic anhydrase family, which catalyzes the rapid interconversion of carbon dioxide and water tobicarbonate and protons, a reversible reaction which occurs relatively slowly in the absence of catalyst. Furthermore, the active siteof nearly all carbonic anhydrases contains a zinc ion; they have been classified as metalloenzymes. At least fivedistinct CA families (?, ?, ?, ? and ?) have been found. These families have no significant a.a sequence resemblance and in just about allcases are considered to be an example of convergent evolution. The ?-CAs have been demonstrated in humans.

Protein Phosphatase 1, Regulatory Subunit 8 (PPP1R8) is the RNA-binding subunit of a key species of protein phosphatase-1 in the nucleus. The PPP1R8 enzyme is an inhibitor subunit of the main nuclear protein phosphatase-1 (PP-1). PPP1R8 has RNA-binding activity however it doesn’t cleave RNA and may target PP-1 to RNA-associated substrates. Two isoforms of the PPP1R8 protein are specific inhibitors of type 1 serine/threonine protein phosphatases which can bind but not cleave RNA. The third isoform of the PPP1R8 protein is deficient in of the phosphatase inhibitory activity nonetheless it is a single-strand endoribonuclease comparable to RNase E of E. coli.

Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.

GNPNAT1 is a member of the GNA1 subfamily of the larger acetyltransferase family of proteins. GNPNAT1 is limited to the Golgi apparatus and the endosome. GNPNAT1 is vital for UDPGlcNAc biosynthesis pathway. GNPNAT1 catalyzes the synthesis of GlcNAc6P from AcCoA and GlcN6P, a step in the UDP-GlcNAc6P formation pathway.

Proteasome subunit alpha type-8 (PSMA8) is a member of the peptidase T1A family. PSMA8 is a multicatalytic proteinase complex which is distinguished by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. The PSMA8 subunit may be testis-specific.

Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.

M2 autoantigen is a key mark of antimitochondrial autoantibodies (AMA), a typical serological feature in patients suffering from primary biliary cirrhosis (PBC) which is a serious autoimmune liver disease accompanied by damage to intrahepatic bile ducts. Molecular definition of the M2 antigen has displayed it as no less than 3 separate target proteins. The M2 role is like the so-called E2 subunits (or dihydrolipoamide transferases) of different mitochondrial dehydrogenase complexes:
*pyruvate dehydrogenase complex.
*branched chain 2-oxo-acid dehydrogenase complex.
*2-oxoglutarate dehydrogenase complex.
Biochemically, these complexes catalyze the oxidative decarboxylation of various alpha-keto-acid substrates and systematically engage with a prosthetic lipoamide group; they are situated in the mitochondrial matrix in association with the inner membrane. The most well-known reactivity of AMA positive PBC sera is against PDC-E2. Some patients have AMA which reacts with PDC-E2 alone (95%), but most patients also show reactivity against OGDC-E2 (39-88%) and/or BCOADC-E2 (53-55%). Actually, patients can be found with reactivity only against OGDC-E2 and/or BCOADC-E2 and no PDC-E2 autoantibodies. These patients will be overlooked in assays based on natural source-derived, predominantly PDC-E2-containing M2 antigen preparations.

ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.

AKR1C1 transfers progesterone to its inactive state or in other words catalyzes the reaction of 20-alpha-hydroxy progesterone (20-alpha-OHP). In the liver and intestine. AKR1C1 transfers bile and monitors the intrahepatic bile acid concentration though it has a low bile-binding ability. AKR1C1 participates in myelin formation. AKR1C1 is part of the aldo/keto reductase superfamily, which has over 40 known enzymes which catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors thus display overlapping but distinct substrate specificity.

Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the sigma class glutathione-S-transferase family. The HPGDS enzyme catalyzes the conversion of PGH2 to PGD2 and has a role in the production of prostanoids in the immune system and mast cells. The presence of the HPGDS enzyme can be utilized to identify the differentiation stage of human megakaryocytes. Furthermore, HPGDS is a prostaglandin involved in smooth muscle contraction/relaxation and an effective inhibitor of platelet aggregation, and the conjugation of glutathione with a extensive range of aryl halides and organic isothiocyanates. In addition, HPGDS displays low glutathione-peroxidase activity towards cumene hydroperoxide. HPGDS is expressed in a number of megakaryocytic cell lines but not in platelets. HPGDS is highly expressed in the adipose tissue, macrophages and placenta; however it is expressed at lower levels in the lung, heart, lymph nodes, appendix, bone marrow and fetal liver.

CCL4L1 (C-C motif chemokine 4-like) is a member of to intercrine beta (chemokine CC) family. The CCL4L1 protein is similar to CCL4 which inhibits HIV replication in peripheral blood monocytes which express CCR5.

Protein Phosphatase 4 Catalytic subunit (PPP4C), is a part of the Serine/threonine-protein phosphatase catalytic subunits which tskes part in dephosphorylation and regulation of HDAC3. The protein phosphatase (PP) holoenzyme is a trimeric complex compound of a regulatory subunit, a variable subunit and a catalytic subunit. 4 major families of protein phosphatase catalytic subunits have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C.

Phosphoribosyl Pyrophosphate Synthetase 2, also known as PRPS2 is a member of the ribose-phosphate pyrophosphokinase family. PRPS2 catalyzes the synthesis of 5-phosphoribosyl 1-pyrophosphate from ATP and D-ribose 5-phosphate.

Sepiapterin Reductase is an aldo-keto reductase that catalyzes the NADPH-dependent reduction of pteridine derivatives and is essential in the biosynthesis of BH4. Mutations in Sepiapterin Reductase gene result in DOPA-responsive dystonia due to sepiaterin reductase deficiency defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Sepiapterin reductase is part of the short-chain dehydrogenase/reductase family which reduces exogenous carbonyl compounds as well as phenylpropanedione. Sepiapterin reductase is an important enzyme for the biosynthesis of tetrahydrobiopterin, an necessary cofactor for aromatic amino acid hydrolases together with tyrosine hydroxylase, the rate-limiting enzyme in DOPA synthesis.

PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.

Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like β-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

PPME1 catalyzes the demethylation and inactivation of protein phosphatase (PP2A), a multimeric phosphoserine/ threonine protein phosphatase related to growth inhibition and cell cycle arrest. PPME1 can demethylate PP2A catalytic subunit in vitro and okadaic acid treatment can inhibit this reaction. It is conserved from yeast to human and holds a motif found in lipases having a catalytic triad activated serine as their active site nucleophile.

Carboxypeptidase A4 (CPA4) belongs to the carboxypeptidase A/B subfamily, and it is located in a cluster with 3 other family members on chromosome 7. CPA4 is a secreted, zinc-dependent metallocarboxypeptidase, which removes the C-terminal amino acid from peptides having a free C-terminal carboxyl group. CPA4 is a metalloprotease which may be involved in the histone hyperacetylation pathway. CPA4 are synthesized as zymogens which are activated by proteolytic cleavage.

ACP1 is part of the phosphotyrosine protein. ACP1 functions as an acid phosphatase and a protein tyrosine phosphatase (PTPase) existing in all human tissues, including adipocytes. ACP1 enzyme hydrolyzes protein tyrosine phosphate to protein tyrosine and orthophosphate, and also orthophosphoric monoesters to alcohol and orthophosphate. ACP1 is present in adipocytes, thus playing a specific role in the regulation of adipose tissue. High levels of the ACP1 negatively regulate cell proliferation and growth of leiomyomas during dephosphorylation of the PDGF receptor. High significant differences in birth weight-placental weight relationships were observed among acid phosphatase locus 1 phenotypes.

DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.

CD33 is putative adhesion molecule of myelomonocytic-derived cells which mediates sialic-acid dependent binding to cells. CD33 prefers to bind to alpha-2,6-linked sialic acid. The sialic acid recognition site is masked by cis interactions with sialic acids on the same cell surface. In the immune response, CD33 perform as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatases through their SH2 domains which block signal transduction through dephosphorylation of signaling molecules. In addition, CD33 induces apoptosis in acute myeloid leukemia.

Glutamine--Fructose-6-Phosphate Transaminase 1 (GFPT1) participates in the hexosamine pathway and controls the glucose fluidity into the hexosamine pathway. GFPT1 regulates the availability of precursors for N- and O-linked glycosylation of proteins. GFPT1 controls the circadian expression of clock genes ARNTL/BMAL1 and CRY1.