PIN1 Antibodies

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1)

Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr- Guru ) motifs. By causing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in several cellular processes (PubMed:21497122, PubMed:22033920, Ref.

21). Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized.

Gene Information

Human
Gene Name:	PIN1
Uniprot:	Q13526
Entrez:	5300

Family

Belongs to:
No superfamily

Alternative Names

dod; EC 5.2.1.8; peptidylprolyl cis/trans isomerase, NIMA-interacting 1; peptidyl-prolyl cis/trans isomerase, NIMA-interacting; peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis-trans isomerase Pin1; Pin1; PPIase Pin1; prolyl isomerase; protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1; protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1; Rotamase Pin1; UBL5

Molecular Weight

Mass (kDA):
18.243 kDA

Genomic Context

Human
Location:	19p13.2
Sequence:	19; NC_000019.10 (9835207..9849689)

Tissue Specificity

The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells.

Subcellular Localizations

Nucleus. Nucleus speckle. Cytoplasm. Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122).

Diseases

• Malignant Neoplasms
• Neoplasms
• Alzheimer's Disease
• Cell Transformation, Neoplastic
• Malignant Neoplasm Of Breast
• Neurodegenerative Disorders
• Nerve Degeneration
• Carcinoma
• Mammary Neoplasms
• Neurofibrillary Tangles
• Neoplasm Metastasis
• Malignant Paraganglionic Neoplasm
• Lung Neoplasms

• Cell Invasion
• Inflammation
• Prostatic Neoplasms
• Malignant Neoplasm Of Lung
• Carcinogenesis
• Dementia
• Adenocarcinoma

Pathways

• Transport
• Auxin Transport
• Auxin Efflux
• Localization
• Cell Cycle
• Mitosis
• Pathogenesis
• Cell Proliferation
• Cell Division
• Cell Growth
• Endocytosis
• Gravitropism
• Cell Death

• Interphase
• Auxin Influx
• Hyperphosphorylation
• Oncogenesis
• Secretion
• Organ Formation
• Protein Folding

PTMs

• Phosphorylation
• Dephosphorylation
• Ubiquitination
• Cleavage
• Ribosylation
• Oxidation
• Acetylation

• Carboxylation
• Isgylation
• Deamination
• Nitration
• Reduction
• Glycosylation
• Methylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/PIN1

Best Uses Of The PIN1 Marker

PIN1 is a phosphorylated Ser/Thr/Pro motif that is responsible for triggering conformational changes in various proteins. In addition , to catalyzing changes in conformation, PIN1 also promotes the proliferation and movement of cells. In this article, we will examine the most effective applications of this marker. This article will show you how to utilize this marker in a variety of biological applications.

PIN1 is a Ser/Thr/Pro-phosphorylated motif

The function of PIN1 is to regulate the activity of protein by regulating phosphorylation and dephosphorylation at the serine/threonine-proline motifs. PIN1 is the only enzyme that isomerises Ser/Thr-Pro peptide bonds. This regulatory mechanism may play a crucial role in the progression of mitotics, the pathogenesis of Alzheimer's disease, and other human diseases.

Pin1 plays an important role in cell proliferative processes and has been demonstrated to be overexpressed in a variety of human tumors. The protein is responsible for regulating cell proliferation during the process of oncogenesis. It is a crucial stage in the development of tumors. Further studies are needed to understand the role of Pin1 in human cancer. This article provides a summary of the current state of the expression of pin1.

Molecular analyses of the human Pin1 protein reveal that the protein exhibits acid-base catalysis. Pin1 prefers to interact with acidic residues near the active site. The basic cluster is comprised of high-quality conserved residues which sequester the sulfate-ion. This suggests that Pin1 targets many mitosis-specific phosphoproteins.

PIN1 is found to be overexpressed in a variety of human breast cancer cells and tissues. Incredibly, the protein's expression is linked to the level of cyclin D1 in cancerous tumors. Pin1 is crucial for the transcriptional activity of the cyclin D1. Similarly, PIN1 is essential for activating c-Jun and the activation of the Ras-dependent signaling pathway.

Moreover, Pin1 is involved in other cell cycle transition points. PIN1 influences key G1/S regulators which include cyclin D1. It can also regulate the upstream regulation of cell cycle checkpoints. Pin1 expression enhances the stability level of cyclin D1 proteins. The increased stability of Pin1 has numerous benefits for cancer treatment, among them.

It facilitates conformational change

TRIP13, which is the lowest-ranking member of the ATPase protein family, is responsible to catalyze the change in the conformation of MAD2. The process of MAD2 disassembly requires a large amount of energy which is released via the breaking of S1/S2 that assists in the refolding of S2. The cleavage of MAD2 is mediated by the ATPase complex.

The pores of TRIP13 are functionally similar to the remodelers of the AAA+ family and share a divergent mechanism. Their positions suggest that they are in contact with the substrate. The structure of TRIP13 suggests AAA domains are in the apo state. Their position also suggests that they played a role in meiotic and mitotic segregation. The precise function of the pores loops is not clear.

It encourages the proliferation of

Proliferative cells refer to an increase in the number of cells due to expansion and division. Proliferation is essential for the maintenance and repair of tissues in the body as well as to protect against damage and disease. Here are a few ways that cell growth can encourage proliferative growth. Learn more about the various kinds of cancer cells and how this can influence the progression of the disease. Also, find out about the most effective ways to boost the proliferation of cells in your body.

It encourages migration

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References

PMID: 8606777 by Lu K.P., et al. A human peptidyl-prolyl isomerase essential for regulation of mitosis.

PMID: 11470801 by Kamimoto T., et al. Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1.